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1000 results found for “Inhibin A”
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Name :
CAMK2N1 HumanDescription:
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 Human Recombinant
PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.
Product # :
PRO-1873Price :
Quantity :
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Shipped with Ice Packs
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Description
CAMK2N1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 10.9kDa. CAMK2N1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAMK2N1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).
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Synonyms
PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEVLPY GDEKLSPYGD GGDVGQIFSC RLQDTNNFFG AGQNKRPPKL GQIGRSKRVV IEDDRIDDVL KNMTDKAPPG V.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
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Shipped at Room temp
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Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
Citations
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MIP 1a MouseDescription:
Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
Product # :
CHM-320Price :
Quantity :
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Shipped at Room temp
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Description
Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 1mg/ml solution containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
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Background
What is the molecular weight/Mw of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein has a total Mw of 7.82kDa.
What is the source or expression system of MIP 1A MOUSE Protein?
Escherichia Coli.
What is the Purity of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A MOUSE Protein?
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of MIP 1A MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
What applications can MIP 1A MOUSE Protein be used in?
MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A MOUSE Protein?
The endotoxin level is minimal, MIP 1A MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL13 HumanDescription:
BCA-1/BLC Human Recombinant (CXCL13)
C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.
Product # :
CHM-348Price :
Quantity :
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Shipped at Room temp
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Description
CXCL13 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 10.3 kDa. The BCA-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCA-1 protein was lyophilized from a concentrated (0.5mg/ml) solution containing 20mM PBS & 150mM NaCl pH-7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human B cells using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
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Introduction
BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.
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Synonyms
C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNG CPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKR SSSTLPVPVFKRKIP.
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Background
What is the molecular weight/Mw of CXCL13 HUMAN Protein?
CXCL13 HUMAN Protein has a total Mw of 10.3kDa.
What is the source or expression system of CXCL13 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL13 HUMAN Protein?
CXCL13 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL13 HUMAN Protein?
Determined by its ability to chemoattract human B cells using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CXCL13 HUMAN Protein?
VLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNG CPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKR SSSTLPVPVFKRKIP.
What applications can CXCL13 HUMAN Protein be used in?
CXCL13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL13 HUMAN Protein?
The endotoxin level is minimal, CXCL13 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL13 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL13 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GOT1 HumanDescription:
Glutamic-Oxaloacetic Transaminase 1 Human Recombinant
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
Product # :
ENZ-528Price :
Quantity :
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Shipped with Ice Packs
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Description
GOT1 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GOT1 Human solution containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
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Synonyms
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A15 MouseDescription:
S100 Calcium Binding Protein A15 Mouse Recombinant
Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.
Product # :
PRO-1145Price :
Quantity :
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Shipped with Ice Packs
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Description
S100A15 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (1-108) and having a molecular mass of 15.0 kDa.S100A15 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The S100A15 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Mouse S100A15 is a protein of 104 amino acids with an expected molecular weight of 12,870 Dalton having 2 EF-hand calcium binding sites. The S100A15 expression is upregulated in cultured keratinocytes stimulated to differentiate by calcium or phorbol esters. S100A15 is expressed in the skin and keratinocytes.
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Synonyms
Protein S100-A7A, S100 calcium-binding protein A15A, S100 calcium-binding protein A7A.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPDTPV EDSLFQIIHC FHHYAAREGD KETLSLEELK ALLLDSVPRF MDTLGRRQPY YITELFRAAD KNKDNQICFD EFLYILGKLV KDYHLQFHRQ LCAHYCTEHS LY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LDHA, E.Coli ActiveDescription:
Lactate Dehydrogenase A, BioActive E.Coli Recombinant
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
Product # :
ENZ-1144Price :
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Shipped with Ice Packs
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Description
LDHA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1 kDa.LDHA E.Coli is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LDHA E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), containing 100mM NaCland 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 200unit/mg. 1 unit converts 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37˚C
Citations
More Info
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Introduction
D-lactate dehydrogenase or ldhA is an enzyme, part of the D-lactate dehydrogenase protein family. IDHA is a cytochrome that enhances the catalyzation of D-lactate dehydrogenase ldhA reaction. This enzyme has 2 substrates ((D) -lactate & ferricytochrome c), thus, it has 2 end products (pyruvate & ferrocytochrome c).
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Synonyms
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAGEA3 HumanDescription:
Melanoma Antigen Family A, 3 Human Recombinant
CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.
Product # :
PRO-502Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAGEA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a.) and having a molecular mass of 37.1kDa.MAGEA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAGEA3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MAGE belongs to the MAGE gene family, that comprises 12 known genes, of which 6 are expressed in tumors. The Melanoma-associated antigen 3 genes were originally isolated from different kinds of tumors, and based on their virtually limited tumor-specific expression in adult tissues, they were used as targets for cancer immunotherapy. MAGEA3 is a tumor-specific antigen extensively expressed in solid and hematologic malignancies, but not in normal tissues, with the exclusion of testis and placenta. Consequently, MAGEA3 is an outstanding candidate tumor antigen.
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Synonyms
CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPLEQRS QHCKPEEGLE ARGEALGLVG AQAPATEEQE AASSSSTLVE VTLGEVPAAE SPDPPQSPQG ASSLPTTMNY PLWSQSYEDS SNQEEEGPST FPDLESEFQA ALSRKVAELV HFLLLKYRAR EPVTKAEMLG SVVGNWQYFF PVIFSKASSS LQLVFGIELM EVDPIGHLYI FATCLGLSYD GLLGDNQIMP KAGLLIIVLA IIAREGDCAP EEKIWEELSV LEVFEGREDS ILGDPKKLLT QHFVQENYLE YRQVPGSDPA CYEFLWGPRA LVETSYVKVL HHMVKISGGP HISYPPLHEW VLREGEE
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SAR1A HumanDescription:
GTP-Binding Protein SAR1A Human Recombinant
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
Product # :
PRO-709Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SAR1A Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids (1- 198 a.a.) and having a molecular mass of 24.5kDa.The SAR1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SAR1A solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.
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Synonyms
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ANXA10 HumanDescription:
Annexin A10 Human Recombinant
Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.
Product # :
PRO-1045Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANXA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-324 a.a.) and having a molecular mass of 39.8kDa.ANXA10 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANXA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Annexin A10 (ANXA10) is a member of the annexin family of calcium-binding proteins that contains a few members which are described by a conserved core domain that binds phospholipids in a Ca2+-dependent manner, and a unique amino-terminal region, which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and might be required in the regulation of cellular growth and signal transduction pathways throughout the cell.
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Synonyms
Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMFCGDY VQGTIFPAPN FNPIMDAQML GGALQGFDCD KDMLINILTQ RCNAQRMMIA EAYQSMYGRD LIGDMREQLS DHFKDVMAGL MYPPPLYDAH ELWHAMKGVG TDENCLIEIL ASRTNGEIFQ MREAYCLQYS NNLQEDIYSE TSGHFRDTLM
NLVQGTREEG YTDPAMAAQD AMVLWEACQQ KTGEHKTMLQ MILCNKSYQQ LRLVFQEFQN ISGQDMVDAI NECYDGYFQE LLVAIVLCVR DKPAYFAYRL YSAIHDFGFH NKTVIRILIA RSEIDLLTIR KRYKERYGKS LFHDIRNFAS GHYKKALLAI CAGDAEDY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFN g AntibodyDescription:
Interferon-gamma, Mouse Anti-Human
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
ANT-123Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Formulation
1mg/ml in PBS (after reconstitution).
Citations
More Info
-
Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. -
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human IFN-g.
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Ig Subclass
Mouse IgG2a.
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Clone
NYRhIFNg.
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Titer
This antibody loses its antigen binding capacity when immobilized on plastic. Biological activity is determined by virus neutralization assay and MHC class II induction.
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
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Purification Method
Ion exchange.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 1RA AntibodyDescription:
Interleukin-1 Receptor Antagonist, Mouse Anti-Human
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
ANT-238Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
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Formulation
1mg/ml in PBS (after reconstitution)
Citations
More Info
-
Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
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Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human IL-1RA.
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Ig Subclass
Mouse IgG2b.
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Clone
NYR-hIL1RA.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation.
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Titer
By direct ELISA, 1:10,000 dilution will yield 0.8 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
-
Purification Method
Ion exchange.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AtosibanDescription:
Atosiban
Product # :
HOR-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Atosiban also called ADH (Anti-Diuretic Hormone) has a molecular formula of C43H67N11O12S2, 3-Mercaptopropionyl-D-Tyr(ET)-Ile-Thr-Asn-Cys-Pro-Orn-Gly-NH2 having a Mw of 994.2 Dalton.
Formulation
The Atosiban peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by analysis by RP-HPLC.
HPLC, MS
Citations
More Info
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Introduction
Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Atosiban although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Atosiban should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Atosiban in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of ATOSIBAN Protein?
ATOSIBAN Protein has a total Mw of 0.99kDa.
What is the Purity of ATOSIBAN Protein?
ATOSIBAN Protein is > 98% pure as determined by SDS-PAGE.
What is the Biological Activity of ATOSIBAN Protein?
The biological functionality of ATOSIBAN Protein will be determined in the future.
What applications can ATOSIBAN Protein be used in?
ATOSIBAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ATOSIBAN Protein?
The endotoxin level is minimal, ATOSIBAN Protein was purified using conventional chromatography techniques.
Who supplies ATOSIBAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of ATOSIBAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LLO PEST freeDescription:
Listeriolysin-O PEST free Recombinant
Listeriolysin-O, LLO, hlyA.
Product # :
PRO-373Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Listeriolysin O s a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. PEST sequence is 19 amino acids peptide located at the protein NH 2-terminus, that targets the toxin for degradation. This motif is essential for bacterial virulence.
Source
Escherichia Coli.
Formulation
The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol and 0.5M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
7x104 HU/mg. 2mM DTT could be use to reactivate the toxin.
Citations
More Info
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Introduction
Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.
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Synonyms
Listeriolysin-O, LLO, hlyA.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AGA Human, sf9Description:
Aspartylglucosaminidase Human Recombinant, sf9
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
Product # :
ENZ-990Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
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Synonyms
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HBsAg ayw, 31kDaDescription:
Hepatitis B Surface Antigen ayw Recombinant
Product # :
HBS-877Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant HbsAg ayw full length is a 31kDa proteincloned from HBV 320 genome and fused to 6xHis Tag.
Source
Escherichia Coli.
Formulation
Sterile Filtered solution (1mg/ml) contains 7.5mM phosphate buffer pH-7.2, 75mM NaCl and 50% glycerol.
Purity
Greater than 99.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV). The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
HBsAg Should be stored at 4°C between 3-4 weeks and for future use should be stored below -18°C.
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Amino Acid Sequence
MGQNLSTSNP LGFFPDHQLD PAFRANTANP DWDFNPNKDT WPDANKVGAG AFGLGFTPPH
GGLLGWSPQA QGILQTLPTN PPPASTNRQS GRQPTPLSPP LRNTHPQAMQ WNSTTFHQTL
QDPRVRGLYF PAGGSSSGTV NPVPTTVSPI SSIFSRIGDP TRILTIPQSL DSWWTSLNFL
GGTTVCLGQN SQSPTSNHSP TSCPPTCGYR WMCLMLPVCP LIPGSSTTTG PCRTCTTPAQ
GTMYPSCCCT KPSDGNCTCP IPSSWAFGKF LWEWASHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PKAkt1/PKBaDescription:
Protein Kinase Akt1/PKB alpha, Active enzyme Human Recombinant
RAC-alpha serine/threonine-protein kinase, EC 2.7.11.1, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, AKT1, AKT, RAC, PRKBA, MGC99656, RAC-ALPHA.
Product # :
PKA-206Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Protein Kinase B is a glycosylated polypeptide having a molecular mass of 59.1 kDa. Recombinant Protein Kinase B is purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PKAkt1 1.9mg/ml, in 50mM NaCl, 1mM DTT, 25mM beta glycerophosphate, 50% glycerol, pH 8.5.
Citations
More Info
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Introduction
Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8. -
Synonyms
RAC-alpha serine/threonine-protein kinase, EC 2.7.11.1, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, AKT1, AKT, RAC, PRKBA, MGC99656, RAC-ALPHA.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Unit Definition
20.000 Units/mg (1 Unit = 1 pmol/min transferred to synthetic peptide RPRAATF at 30 degree Celsius). No protease activity detectable.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Apolipoprotein A1 HumanDescription:
Apolipoprotein A-I Human Recombinant
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
Product # :
CYT-750Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Apolipoprotein A-I Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids and having a molecular mass of 28.1kDa.The APOA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The APOA1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
APOA1 (Apolipoprotein A-1) is a human protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
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Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, APOA1, MGC117399.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Apolipoprotein A-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOA1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized APOA1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
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Background
Apolipoprotein A-I Human Recombinant: A Promising Therapeutic Agent for Cardiovascular Diseases
Abstract:
Cardiovascular diseases (CVDs) remain a leading cause of mortality worldwide. Dyslipidemia, characterized by abnormal lipid profiles, is a significant risk factor for the development of CVDs. Apolipoprotein A-I (ApoA-I) is the primary protein component of high-density lipoprotein (HDL), known as the "good cholesterol." ApoA-I plays a crucial role in reverse cholesterol transport, promoting the efflux of cholesterol from peripheral tissues to the liver for elimination. Recombinant ApoA-I offers a potential therapeutic strategy for enhancing HDL functionality and reducing CVD risk. This research paper aims to provide an overview of ApoA-I human recombinant, its production methods, and its therapeutic applications in cardiovascular medicine.Introduction
Cardiovascular diseases and dyslipidemia
Role of apolipoprotein A-I in reverse cholesterol transport
Potential of ApoA-I human recombinant as a therapeutic agentStructure and Function of Apolipoprotein A-I
Primary structure and domains of ApoA-I
Functional properties of ApoA-I in reverse cholesterol transport
Interaction with other lipoproteins and cellular receptorsProduction of Apolipoprotein A-I Human Recombinant
Expression systems for recombinant ApoA-I
Biotechnological methods for large-scale production
Purification and characterization of recombinant ApoA-ITherapeutic Applications of Apolipoprotein A-I Human Recombinant
Promotion of reverse cholesterol transport
Anti-inflammatory and antioxidant effects
Enhancement of endothelial function
Cardioprotective effects in animal modelsClinical Trials and Future Perspectives
Phase I and II clinical trials
Challenges and limitations
Future directions and potential therapeutic combinationsConclusion
Summary of the potential of ApoA-I human recombinant as a therapeutic agent for CVDs
Importance of ongoing research and clinical trialsWhat is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein has a total Mw of 28.1kDa.
What is the source or expression system of APOLIPOPROTEIN A1 Protein?
Escherichia Coli.
What is the Purity of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.
What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
DEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ.
What applications can APOLIPOPROTEIN A1 Protein be used in?
APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
The endotoxin level is minimal, APOLIPOPROTEIN A1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CFI HumanDescription:
Complement Factor I Human
Complement factor I, C3B/C4B inactivator, CFI, IF.
Product # :
PRO-2701Price :
Quantity :
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Shipped with Ice Packs
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Description
Human Complement Factor I produced in Human plasma is glycosylated polypeptide composed of 2 disulfide-linked chains having a total molecular mass of 88kDa.
Source
Human Plasma.
Formulation
CFI protein solution contains Sodium phosphate, pH 7.2.
Purity
Greater than 93.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CFI cleaves and inactivates C3b and C4b. CFI is inactive without a cofactor such as the soluble factor H and C4b binding protein. CFI cleaves the alpha-peptide chain of C3b and C4b when these binds1 of the cofactors. This cleavage inactivates all of the complement activating functions of these proteins producing iC3b and iC4b.CFI cleaves the alpha chain of C3b twice and this releases a small fragment called C3f. CFI can cleave iC3b releasing C3c from C3dg in the presence of CR1.C4b is cleaved rapidly at 2 sites separating C4c from C4d.
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Synonyms
Complement factor I, C3B/C4B inactivator, CFI, IF.
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Physical Appearance
Sterile filtered solution.
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Stability
CFI Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL1A PorcineDescription:
Interleukin-1 Alpha Porcine Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
Product # :
CYT-396Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.Citations
More Info
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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.
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Background
What is the molecular weight/Mw of IL1A PORCINE Protein?
IL1A PORCINE Protein has a total Mw of 18kDa.
What is the source or expression system of IL1A PORCINE Protein?
Escherichia Coli.
What is the Purity of IL1A PORCINE Protein?
IL1A PORCINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1A PORCINE Protein?
The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.
What is the amino acid sequence of IL1A PORCINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.
What applications can IL1A PORCINE Protein be used in?
IL1A PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1A PORCINE Protein?
The endotoxin level is minimal, IL1A PORCINE Protein was purified using conventional chromatography techniques.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GH Antagonist ChickenDescription:
Growth Hormone Antagonist Chicken Recombinant
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-538Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Somatotropin Chicken Antagonist Recombinant mutein G119R produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids with an additional Ala at the N-terminus and having a molecular mass of 22.3 kDa. The Chicken Growth-Hormone Antagonist Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3 pH-8.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Recombinant Chicken Growth Hormone G119R mutant did not bind to ovine GHR-ECD and was devoid of any biological activity in FDC-P1 3B9 cells.
However, in binding experiments that were carried out using chicken liver membranes, both ovine GH and chicken GH showed similar IC50 values in competition with 125I-ovine GH, while the IC50 of G119R mutein was 10-fold higher.
These results emphasize the importance of species specificity and indicate the possibility of antagonistic activity of chGH G119R in homologous system.Citations
More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth-Hormone Chicken antagonist although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Growth-Hormone Chicken antagonist in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.
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Protein content
Protein quantitation was carried out by: UV spectroscopy at 280 nm using the absorbency value of 0.74 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Influenza-B Paired AntibodyDescription:
Mouse Anti Influenza-B Paired
Product # :
ANT-652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Influenza-B conjugation antibody and Influenza-B coating antibody are used to develop rapid test for Influenza-B rapid test. Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).
Formulation
* Influenza-B conjugation antibody in PBS, PH 7.4 .
* Influenza-B coating antibody in PBS, PH 7.4 .Purity
Greater than 90%.
Citations
More Info
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Introduction
Influenza-B virus is a genus in the virus family Orthomyxoviridae. The only species in this genus is called "Influenza B virus". Influenza B virus only infects humans and seals. This limited host range is apparently in contrast with those caused by the similar Influenza virus A as both mutate by both genetic drift and reassortment. Influenza-B virus evolves slower than A viruses and faster than C viruses. Influenza-B virus mutates at a rate 2-3 times lower than type A. However, influenza B mutates enough that lasting immunity is not possible. The Influenza B virus capsid is enveloped while its virion consists of a matrix protein + envelope + nucleoprotein complex + nucleocapsid, and a polymerase complex. Influenza B is sometimes spherical and sometimes filamentous. Its 500 or so surface projections are made of hemagglutinin and neuraminidase.
The Influenza B virus is 14648 nucleotides long and consists of eight segments of linear negative-sense, single-stranded RNA. The multipartite genome is encapsidated, each segment in a separate nucleocapsid, and the nucleocapsids are surrounded by one envelope. -
Physical Appearance
2 vials of sterile Filtered clear colorless solution.
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Stability
For periods up to 1 month Influenza-B Paired Antibody should be stored at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Applications
Lateral flow immunoassay.
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Type
Mouse antibody Monoclonal.
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Purification Method
Purified monoclonal IgG2b by protein A chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A7A HumanDescription:
S100 Calcium Binding Protein A7A Human Recombinant
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
Product # :
PRO-756Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
S100A7A takes part in epidermal differentiation and inflammation thus is significant for the pathogenesis of psoriasis and other diseases.
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Synonyms
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
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Stability
Store lyophilized S100A7A Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted S100A7A can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add pyrogen free water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MMKHHHHHHASNTQAERSIIG MIDMFHKYTG RDGKIEKPSL LTMMKENFPN FLSACDKKGI HYLATVFEKK DKNEDKKIDF SEFLSLLGDI AADYHKQSHG AAPCSGGSQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Apolipoprotein A1 MouseDescription:
Apolipoprotein A-I Mouse Recombinant
Apolipoprotein A-I, Apo-AI, ApoA-I, Apolipoprotein A1, ProapoA-I.
Product # :
CYT-891Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
APOA1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (25-264a.a) and having a molecular mass of 30.3kDa.APOA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APOA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
APOA1 (Apolipoprotein A-1) is a protein with a specific role in lipid metabolism being the main protein component of HDL in the plasma. APOA1 promotes cholesterol efflux from tissues to the liver for excretion. Furthermore, APOA1 is a cofactor for LCAT, which is responsible for the formation of most plasma cholesteryl esters. In addition, APOA1 activates spermatozoa motility as part of the SPAP complex. The APOA1 gene is strongly linked with two other apolipoprotein genes on chromosome 11. Defects in the APOA1 gene are linked to HDL deficiency including Tangier disease, and with systemic non-neuropathic amyloidosis. High levels of APOA1 are linked to the manifestation of asthma and atopy.
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Synonyms
Apolipoprotein A-I, Apo-AI, ApoA-I, Apolipoprotein A1, ProapoA-I.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDEPQSQW DKVKDFANVY VDAVKDSGRD YVSQFESSSL GQQLNLNLLE NWDTLGSTVS QLQERLGPLT RDFWDNLEKE TDWVRQEMNK DLEEVKQKVQ PYLDEFQKKW KEDVELYRQK VAPLGAELQE SARQKLQELQ GRLSPVAEEF RDRMRTHVDS LRTQLAPHSE QMRESLAQRL AELKSNPTLN EYHTRAKTHL KTLGEKARPA LEDLRHSLMP MLETLKTQVQ SVIDKASETL TAQ.
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Background
What is the molecular weight/Mw of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein has a total Mw of 30.3kDa.
What is the source or expression system of APOLIPOPROTEIN A1 Protein?
Escherichia Coli.
What is the Purity of APOLIPOPROTEIN A1 Protein?
APOLIPOPROTEIN A1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APOLIPOPROTEIN A1 Protein?
The biological functionality of APOLIPOPROTEIN A1 Protein will be determined in the future.
What is the amino acid sequence of APOLIPOPROTEIN A1 Protein?
MGSSHHHHHH SSGLVPRGSH MGSDEPQSQW DKVKDFANVY VDAVKDSGRD YVSQFESSSL GQQLNLNLLE NWDTLGSTVS QLQERLGPLT RDFWDNLEKE TDWVRQEMNK DLEEVKQKVQ PYLDEFQKKW KEDVELYRQK VAPLGAELQE SARQKLQELQ GRLSPVAEEF RDRMRTHVDS LRTQLAPHSE QMRESLAQRL AELKSNPTLN EYHTRAKTHL KTLGEKARPA LEDLRHSLMP MLETLKTQVQ SVIDKASETL TAQ.
What applications can APOLIPOPROTEIN A1 Protein be used in?
APOLIPOPROTEIN A1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOLIPOPROTEIN A1 Protein?
The endotoxin level is minimal, APOLIPOPROTEIN A1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.