Recombinant Mouse Ephrin-B1 Protein (His Tag)
Name :
Recombinant Mouse Ephrin-B1 Protein (His Tag)
Biological Activity :
Background :
Ephrin-B1 also known as EFNB1, is a member of the ephrin family. The transmembrane- associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB1 and B class Eph receptors provide positional cues required for the normal morphogenesis of skeletal elements. Another malformation, preaxial polydactyly, was exclusively seen in heterozygous females in which expression of the X-linked ephrinB1 gene was mosaic, so that ectopic EphB-ephrinB1 interactions led to restricted cell movements and the bifurcation of digital rays.
Biological Activity :
Measured by its ability to compete with mouse EphrinB1 / Fc for binding to immobilized mouse EphB3 in a functional ELISA assay.
Expression Host :
Mouse
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_034240.1
NCBI Gene ID :
Synonyms :
Synonyms :
ephrin-B1
Amino Acid Sequence :
Molecular Weight :
The secreted recombinant mouse EFNB1 consists of 211 amino acids and has a predicted molecular mass of 23.3 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmEFNB1 is approximately 33-38 kDa due to glycosylation.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the mouse EFNB1 (NP_034240.1) extracellular domain (Met 1-Ser 229) was expressed, fused with a polyhistidine tag at the C-terminus.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
Cek5-L Protein, Mouse; EFL-3 Protein, Mouse; Elk-L Protein, Mouse; Epl2 Protein, Mouse; Eplg2 Protein, Mouse; LERK-2 Protein, Mouse; Lerk2 Protein, Mouse; Stra1 Protein, Mouse Ephrin-B1 背景信息 Ephrin-B1 also known as EFNB1, is a member of the ephrin family. The transmembrane- associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB1 and B class Eph receptors provide positional cues required for the normal morphogenesis of skeletal elements. Another malformation, preaxial polydactyly, was exclusively seen in heterozygous females in which expression of the X-linked ephrinB1 gene was mosaic, so that ectopic EphB-ephrinB1 interactions led to restricted cell movements and the bifurcation of digital rays.
References & Citations :
Davy A, et al. (2004) Ephrin-B1 forward and reverse signaling are required during mouse development. Genes Dev. 18(5): 572-83.Compagni A, et al. (2003) Control of skeletal patterning by ephrinB1-EphB interactions. Dev Cell. 5(2): 217-30.Wieland I, et al. (2004) Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome. Am J Hum Genet. 74(6): 1209-15.
MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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Recombinant Mouse Aminoacylase 1 Protein (His Tag)
Name :
Recombinant Mouse Aminoacylase 1 Protein (His Tag)
Biological Activity :
Background :
Aminoacylase 1 (ACY1), a metalloenzyme that removes amide-linked ACY1 groups from amino acids and may play a role in regulating responses to oxidative stress. Both the C-terminal fragment found in the two-hybrid screen and full-length ACY1 co-immunoprecipitate with SphK1. Though both C-terminal and full-length proteins slightly reduce SphK1 activity measured in vitro, the C-terminal fragment inhibits while full-length ACY1 potentiates the effects of SphK1 on proliferation and apoptosis. It suggested that ACY1 physically interacts with SphK1 and may influence its physiological functions. As a homodimeric zinc-binding enzyme, Aminoacylase 1 catalyzes the hydrolysis of N alpha-acylated amino acids. Deficiency of Aminoacylase 1 due to mutations in the Aminoacylase 1 (ACY1) gene follows an autosomal-recessive trait of inheritance and is characterized by accumulation of N-acetyl amino acids in the urine.
Biological Activity :
Measured by its ability to cleave N-acetyl-L-Methione (Ac-Met)
. The specific activity is >4,000 pmoles/min/μg.
Expression Host :
Mouse
Source :
HEK293 Cells
Tag :
Protein Accession No. :
Q99JW2
NCBI Gene ID :
Synonyms :
Synonyms :
aminoacylase 1
Amino Acid Sequence :
Molecular Weight :
The recombinant mouse ACY1 consists of 402 amino acids and has a calculated molecular mass of 45 kDa as estimated by SDS-PAGE under reducing conditions.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the mouse ACY1 (Q99JW2) (Met 1-Ser 408) was expressed with a C-terminal polyhistidine tag.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
1110014J22Rik Protein, Mouse; Acy-1 Protein, Mouse Aminoacylase 1 背景信息 Aminoacylase 1 (ACY1), a metalloenzyme that removes amide-linked ACY1 groups from amino acids and may play a role in regulating responses to oxidative stress. Both the C-terminal fragment found in the two-hybrid screen and full-length ACY1 co-immunoprecipitate with SphK1. Though both C-terminal and full-length proteins slightly reduce SphK1 activity measured in vitro, the C-terminal fragment inhibits while full-length ACY1 potentiates the effects of SphK1 on proliferation and apoptosis. It suggested that ACY1 physically interacts with SphK1 and may influence its physiological functions. As a homodimeric zinc-binding enzyme, Aminoacylase 1 catalyzes the hydrolysis of N alpha-acylated amino acids. Deficiency of Aminoacylase 1 due to mutations in the Aminoacylase 1 (ACY1) gene follows an autosomal-recessive trait of inheritance and is characterized by accumulation of N-acetyl amino acids in the urine.
References & Citations :
Sommer A, et al. (2011) The molecular basis of aminoacylase 1 deficiency. Biochim Biophys Acta. 1812(6): 685-90.Maceyka M, et al. (2004) Aminoacylase 1 is a sphingosine kinase 1-interacting protein. FEBS Lett. 568(1-3): 30-4.Cook RM, et al.(1993) Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. J Biol Chem. 268(23): 17010-7.
MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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Recombinant Mouse Carbonic Anhydrase XIV/CA14 Protein (His Tag)
Name :
Recombinant Mouse Carbonic Anhydrase XIV/CA14 Protein (His Tag)
Biological Activity :
Background :
The Carbonic Anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The Carbonic Anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. CAXIV is a member of CA family that showed an overall similarity of 29–46% to other active CA isozymes. The highest percentage similarity was with a transmembrane CA isoform, CAXII. The CAXIV was found high concentrations in human heart, brain, liver, and skeletal muscle but lower in the colon, small intestine, urinary bladder, and kidney. No CAXIV mRNA was seen in the salivary gland and pancreas. CAXIV is a likely candidate for the extracellular CA postulated to have an important role in modulating excitatory synaptic transmission in brain.
Biological Activity :
Measured by its esterase activity. The specific activity is >400 pmoles/min/μg, as measured with 1 mM 4-Nitrophenyl acetate and 0.8 μg enzyme at 400 nm in 100 μL of 12.5 mM Tris, 75 mM NaCl, pH 7.5.
Expression Host :
Mouse
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_035927.1
NCBI Gene ID :
Synonyms :
Synonyms :
Carbonic Anhydrase XIV
Amino Acid Sequence :
Molecular Weight :
The recombinant mouse CA14 consists of 286 amino acids and has a calculated molecular mass of 32.2 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 45-48 kDa protein in SDS-PAGE under reducing conditions.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the extracellular domain of mouse CA14 (NP_035927.1) (Met 1-Met 290) was expressed with a C-terminal polyhistidine tag.
Buffer Solution :
Lyophilized from sterile 25mM Tris, 0.15mM NaCl, pH 7.5Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
Ca14 Protein, Mouse; Car14 Protein, Mouse; Catm Protein, Mouse Carbonic Anhydrase XIV/CA14 背景信息 The Carbonic Anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The Carbonic Anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. CAXIV is a member of CA family that showed an overall similarity of 29–46% to other active CA isozymes. The highest percentage similarity was with a transmembrane CA isoform, CAXII. The CAXIV was found high concentrations in human heart, brain, liver, and skeletal muscle but lower in the colon, small intestine, urinary bladder, and kidney. No CAXIV mRNA was seen in the salivary gland and pancreas. CAXIV is a likely candidate for the extracellular CA postulated to have an important role in modulating excitatory synaptic transmission in brain.
References & Citations :
Lehtonen J, et al. (2004) Characterization of CA XIII, a Novel Member of the Carbonic Anhydrase Isozyme Family. The Journal of Biological Chemistry. 279: 2719-27.Lindskog S. (1997) Structure and mechanism of Carbonic Anhydrase. Pharmacology & Therapeutics. 74(1)：1-20.Parkkila S, et al. (2001) Expression of membrane-associated Carbonic Anhydrase XIV on neurons and axons in mouse and human brain. PNAS. 98(4): 1918-23.
MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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Influenza B (B/Yamagata/16/1988) Hemagglutinin / HA Protein (ECD, His Tag)
Name :
Influenza B (B/Yamagata/16/1988) Hemagglutinin / HA Protein (ECD, His Tag)
Biological Activity :
Background :
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells’ sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
Biological Activity :
Measured by its ability to agglutinate guinea pig red blood cells. HA titer is 1-10 μg/mL for 1%GRBC
Expression Host :
Influenza B
Source :
Baculovirus-Insect Cells
Tag :
Protein Accession No. :
NCBI Gene ID :
Synonyms :
Synonyms :
Harvey rat sarcoma viral oncogene homolog
Amino Acid Sequence :
Molecular Weight :
The recombinant hemagglutinin of Influenza B virus (B/Yamagata/16/1988) consists 542 amino acids and predicts a molecular mass of 59 kDa.
Purity :
> 95 % as determined by SDS-PAGE.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.
Protein Construction :
A DNA sequence encoding the Influenza B virus (B/Yamagata/16/1988) hemagglutinin (Met1-Thr546), termed as HA, was expressed with a polyhistidine tag at the C-terminus.
Buffer Solution :
Lyophilized from sterile 20 mM Tris, 500 mM NaCl, 10 % glycerol, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
References & Citations :
White JM, Hoffman LR, Arevalo JH, et al. Attachment and entry of influenza virus into host cells. Pivotal roles of hemagglutinin. In Chiu W, Burnett RM, Garcea RL. Structural Biology of Viruses.1997Suzuki Y.Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol. Pharm. Bull. 2005. Senne DA, Panigrahy B, Kawaoka Y, et al. Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential. Avian Dis. 1996Donald J. Benton,Influenza hemagglutinin membrane anchor,PNAS,2018
MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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CA125/MUC16 Protein
Name :
CA125/MUC16 Protein
Description :
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.Binding to MSLN mediates heterotypic cell adhesion. This may contribute to the metastasis of ovarian cancer to the peritoneum by initiating cell attachment to the mesothelial epithelium via binding to MSLN.
Species :
Human
Uniprotkb :
HEK293
Tag :
C-His-Avi
Synonyms :
CA125, CA-125, MUC16, FLJ14303, CA125MUC-16
Construction :
Recombinant Biotinylated Human CA125/MUC16 Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus. It contains Gly12660-Met12923.[Accession |Q8WXI7]
Protein Purity :
> 95% as determined by Tris-Bis PAGE
Molecular Weight :
The protein has a predicted MW of 31.3 kDa. Due to glycosylation, the protein migrates to 52-80 kDa based on Tris-Bis PAGE result.
Endotoxin :
Less than 1EU per μg by the LAL method.
Formulatione :
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Stability & Storage :
-20 to -80°C for 12 months as supplied from date of receipt. -20 to -80°C for 3-6 months in unopened state after reconstitution. 2-8°C for 2-7 days after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background :
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.Binding to MSLN mediates heterotypic cell adhesion. This may contribute to the metastasis of ovarian cancer to the peritoneum by initiating cell attachment to the mesothelial epithelium via binding to MSLN.
References and Literature :
1. Das S , Batra S K. Understanding the Unique Attributes of MUC16 (CA125): Potential Implications in Targeted Therapy[J]. Cancer Research, 2015:0008-5472.CAN-15-1050.2. Rao T D , Park K J , Smith-Jones P , et al. Novel Monoclonal Antibodies Against the Proximal (Carboxy-Terminal) Portions of MUC16[J]. Applied immunohistochemistry & molecular morphology: AIMM / official publication of the Society for Applied Immunohistochemistry, 2010, 18(5):462-472.
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