Search results
1000 results found for “receptor activity-modifying protein”
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Name :
GrpE E.ColiDescription:
HSP-70 Cofactor (HSP24) E.Coli Recombinant
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
Product # :
HSP-014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
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Synonyms
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
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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
MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.
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 :
CDNF RatDescription:
CDNF Rat Recombinant
Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.
Product # :
CYT-730Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CDNF Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.8kDa.The CDNF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.More Info
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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the 6-hydroxy (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
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Synonyms
Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF 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 CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.
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Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.8kDa.
What is the source or expression system of CDNF Protein?
Escherichia Coli.
What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CDNF Protein?
CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.
What is the amino acid sequence of CDNF Protein?
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.
What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF 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 :
Shipping Method :
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.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 :
NMRAL1 HumanDescription:
NmrA-Like Family Domain Containing 1 Human Recombinant
NmrA-like family domain containing protein 1, short chain dehydrogenase/reductase family 48A member 1, HSCARG, SDR48A1, FLJ25918.
Product # :
PRO-1131Price :
Quantity :
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Shipped with Ice Packs
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Description
NMRAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 323 amino acids (1-299) and having a molecular mass of 35.9 kDa.NMRAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NMRAL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
NMRAL1 is a redox sensor protein which goes through reformation and subcellular rearrangement in reaction to alterations in intracellular NADPH/NADP+ levels. When the NADPH concentration is low the protein is found mostly as a monomer, and binds argininosuccinate synthase (ASS1), which takes part in nitric oxide synthesis. Association with ASS1 defects NMRAL1 activity and diminishes the production of nitric oxide, which then inhibits apoptosis. When the NADPH concentration is normal , the protein is found as a dimer and hides the binding site for ASS1.
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Synonyms
NmrA-like family domain containing protein 1, short chain dehydrogenase/reductase family 48A member 1, HSCARG, SDR48A1, FLJ25918.
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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 MGSHMVDKKL VVVFGGTGAQ GGSVARTLLE DGTFKVRVVT RNPRKKAAKE LRLQGAEVVQ GDQDDQVIME LALNGAYATF IVTNYWESCS QEQEVKQGKL LADLARRLGL HYVVYSGLEN IKKLTAGRLA AAHFDGKGEV EEYFRDIGVP MTSVRLPCYF ENLLSHFLPQ KAPDGKSYLL SLPTGDVPMD GMSVSDLGPV VLSLLKMPEK YVGQNIGLST CRHTAEEYAA LLTKHTRKVV HDAKMTPEDY EKLGFPGARD LANMFRFYAL RPDRDIELTL RLNPKALTLD QWLEQHKGDF NLL
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 :
ANXA2Description:
Annexin A2 Human Recombinant
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
Product # :
PRO-777Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANXA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 376 amino acids (1-339a.a.) and having a molecular mass of 42.8 kDa. ANXA2 is fused to a 37 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANXA2 (0.5mg/ml) solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
ANXA2 is part of the annexin family and is involved in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein functions as an autocrine factor which increases osteoclast formation and bone resorption. ANXA2 is associated with sickle cell osteonecrosis. Reduced ANXA2 expression is associated with osteosarcoma metastases. ANXA2 is part of the putative cell surface vitamin D binding protein binding site complex and functions to mediate the chemotactic cofactor effect. ANXA2 is involved in dysferlin deficiency and in muscular dystrophies. Human colon adenocarcinoma cell differentiation is related with an up-regulation of ANXA2.
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Synonyms
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMST VHEILCKLSL EGDHSTPPSA YGSVKAYTNF DAERDALNIE TAIKTKGVDE VTIVNILTNR SNAQRQDIAF AYQRRTKKEL ASALKSALSG HLETVILGLL KTPAQYDASE LKASMKGLGT DEDSLIEIIC SRTNQELQEI NRVYKEMYKT DLEKDIISDT SGDFRKLMVA LAKGRRAEDG SVIDYELIDQ DARDLYDAGV KRKGTDVPKW ISIMTERSVP HLQKVFDRYK SYSPYDMLES IRKEVKGDLE NAFLNLVQCI QNKPLYFADR LYDSMKGKGT RDKVLIRIMV SRSEVDMLKI RSEFKRKYGK SLYYYIQQDT KGDYQKALLY LCGGDD.
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 :
CALB2 HumanDescription:
Calbindin-2 Human Recombinant
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
Product # :
PRO-401Price :
Quantity :
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Shipped with Ice Packs
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Description
CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.
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Synonyms
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
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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 MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.
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 :
PNOC HumanDescription:
Prepronociceptin Human Recombinant
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
Product # :
PRO-1442Price :
Quantity :
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Shipped with Ice Packs
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Description
PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. PNOC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
PNOC protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.
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Synonyms
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
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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 MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.
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 :
RLN2 HumanDescription:
Relaxin-2 Human Recombinant
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Product # :
PRO-1327Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RLN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
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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 MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.
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 :
DNAJC24 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 24 Human Recombinant
DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.
Product # :
HSP-056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DNAJC24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-149 a.a.) and having a molecular mass of 19.5kDa. DNAJC24 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC24 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DnaJ homolog subfamily C member 24 (DNAJC24) belongs to the ZCSL family of proteins and each contain one DPH-type zinc finger. DNAJC24 is involved in the synthesis of diphthamide, a protein found on translation elongation factor EF-2 which is the target of bacterial ADP-ribosylating toxins. DNAJC24 stimulates the ATPase activity of few Hsp70-type chaperones. DNAJC24 detected in heart, brain, spleen, lung, liver, kidney and testis.
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Synonyms
DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.
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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 MGSMMAVEQM PKKDWYSILG ADPSANISDL KQKYQKLILM YHPDKQSTDV PAGTVEECVQ KFIEIDQAWK ILGNEETKRE YDLQRCEDDL RNVGPVDAQV YLEEMSWNEG DHSFYLSCRC GGKYSVSKDE AEEVSLISCD TCSLIIELLH YN.
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 :
JTB HumanDescription:
Jumping Translocation Breakpoint Human Recombinant
Protein JTB, Jumping translocation breakpoint protein, Prostate androgen-regulated protein, PAR protein, Jumping Translocation Breakpoint, JTB, Jumping translocation breakpoint, hJT, HJTB, HSPC222, PAR.
Product # :
PRO-2059Price :
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Shipped with Ice Packs
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Description
JTB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (31-105 a.a.) and having a molecular mass of 10.7kDa.JTB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
JTB protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Jumping Translocation Breakpoint (JTB) takes part in the regulation of cell proliferation and is essential for cytokinesis during mitosis. JTB inhibits apoptosis induced by TGFB1 and increases AURKB activity. JTB is also a part of the chromosomal passenger complex (CPC) which is a key regulator of mitosis.
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Synonyms
Protein JTB, Jumping translocation breakpoint protein, Prostate androgen-regulated protein, PAR protein, Jumping Translocation Breakpoint, JTB, Jumping translocation breakpoint, hJT, HJTB, HSPC222, PAR.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEAPVQEE KLSASTSNLP CWLVEEFVVA EECSPCSNFR AKTTPECGPT GYVEKITCSS SKRNEFKSCR SALMEQRL.
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 :
AGR3 HumanDescription:
Anterior Gradient Protein 3 Homolog Human Recombinant
Anterior gradient protein 3 homolog, AG-3, AG3, hAG-3, Breast cancer membrane protein 11, AGR3, BCMP11, UNQ642/PRO1272, HAG3, PDIA18.
Product # :
PRO-242Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AGR3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-166 a.a) and having a molecular mass of 19.5kDa.AGR3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AGR3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Anterior gradient protein 3 homolog precursor (AGR3) is a secreted cytoplasmic protein that is involved in metastasis induction and p53 tumor suppressor inhibition. AGR3 may function as molecular marker and potential therapeutic target for hormone-responsive breast tumors.
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Synonyms
Anterior gradient protein 3 homolog, AG-3, AG3, hAG-3, Breast cancer membrane protein 11, AGR3, BCMP11, UNQ642/PRO1272, HAG3, PDIA18.
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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 MGSMIAIKKE KRPPQTLSRG WGDDITWVQT YEEGLFYAQK SKKPLMVIHH LEDCQYSQAL KKVFAQNEEI QEMAQNKFIM LNLMHETTDK NLSPDGQYVP RIMFVDPSLT VRADIAGRYS NRLYTYEPRD LPLLIENMKK ALRLIQSEL.
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 :
HCST HumanDescription:
Hematopoietic Cell Signal Transducer Human Recombinant
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
Product # :
PRO-2522Price :
Quantity :
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Description
HCST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 271 amino acids (20-48 a.a.) and having a molecular mass of 30.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).HCST is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HCST protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HCST (Hematopoietic Cell Signal Transducer) is part of the DAP10 family. HCST is capable of being a part of an immunoreceptor complex. HCST takes a vital part in inducing cytotoxicity against MHC class I chain-associated MICA & target cells expressing cell surface ligands such as UL16-binding protein (ULBP) & MICB. HCST complex participates in proliferation as well as cell survival by activating T & NK cell responses.
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Synonyms
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
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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
ADPTTPGERS SLPAFYPGTS GSCSGCGSLS LPLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
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 :
SHBG HumanDescription:
Sex Hormone-Binding Globulin Human Recombinant
Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.
Product # :
PRO-1603Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SHBG Human Recombinant produced in CHO cells is a single, glycosylated, polypeptide chain containing a total of 428 amino acids, having a molecular mass of 46.79kDa (calculated), the SHBG is fused to a 6 a.a C-terminal His tag and also includes a myc-epitope.The Human SHBG is purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
SHBG filtered solution at a concentration of 55.6µg/ml in certified FBS (Fetal Bovine Serum 5%).
More Info
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Introduction
Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.
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Synonyms
Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.
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Physical Appearance
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
AAQPARRARR TKLLLLLLLL LRHTRQGWAL RPVLPTQSAH DPPAVHLSNG PGQEPIAVMT FDLTKITKTS SSFEVRTWDP EGVIFYGDTN PKDDWFMLGL RDGRPEIQLH NHWAQLTVGA GPRLDDGRWH QVEVKMEGDS VLLEVDGEEV LRLRQVSGPL TSKRHPIMRI ALGGLLFPAS NLRLPLVPAL DGCLRRDSWL DKQAEISASA PTSLRSCDVE SNPGIFLPPG TQAEFNLRDI PQPHAEPWAF SLDLGLKQAA GSGHLLALGT PENPSWLSLH LQDQKVVLSS GSGPGLDLPL VLGLPLQLKL SMSRVVLSQG SKMKALALPP LGLAPLLNLW AKPQGRLFLG ALPGEDSSTS FCLNGLWAQG QRLDVDQALN RSHEIWTHSC PQSPGNGTDA SHSRGGPEQKLISEEDLNSA VDHHHHHH.
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 :
RPS5 HumanDescription:
Ribosomal Protein S5 Human Recombinant
40S ribosomal protein S5, S5, RPS5.
Product # :
PRO-1300Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RPS5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a.) and having a molecular mass of 25.3kDa.RPS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RPS5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
40S ribosomal protein S5 (RPS5) is a ribosomal protein, which is a member of the ribosomal protein S7P family.Ribosomes, which are the organelles that catalyze protein synthesis, composed of a small subunit and a large subunit that comprise of over 80 distinct ribosomal proteins. RPS5 is a 204 amino acid component of the 40S complex. RPS5 proteins exist as multiple processed pseudogenes which are scattered throughout the genome. RPS5 is expressed at varying amounts in colorectal cancer cells, proposing a possible role in carconigenesis.
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Synonyms
40S ribosomal protein S5, S5, RPS5.
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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 MGSMTEWETA APAVAETPDI KLFGKWSTDD VQINDISLQD YIAVKEKYAK YLPHSAGRYA AKRFRKAQCP IVERLTNSMM MHGRNNGKKL MTVRIVKHAF EIIHLLTGEN PLQVLVNAII NSGPREDSTR IGRAGTVRRQ AVDVSPLRRV NQAIWLLCTG AREAAFRNIK TIAECLADEL INAAKGSSNS YAIKKKDELE RVAKSNR.
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 :
RAP2B HumanDescription:
RAP2B, Member RAS Oncogene Family Human Recombinant
RAP2B, member of RAS oncogene family, Ras-related protein Rap-2b, Ras Family Small GTP Binding Protein RAP2B2, Small GTP Binding Protein.
Product # :
PRO-1364Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RAP2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183 a.a) and having a molecular mass of 22.9kDa. RAP2B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RAP2B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ras-related protein Rap-2b (RAP2B) is a part of RAS-related genes family. RAP2B has a threonine residue at aa 61Unlike normal ras proteins which have a nontransforming glutamine residue at that position. The threonine residue makes the intrinsic GTPase activity for Rap2B lower, by this means allows RAP2B to exist in the activated state for a longer period of time than normal ras proteins. RAP2B is a platelet protein which is activated by thrombin and involved in platelet activation. RAP2B may be a candidate oncogene which takes part in carcinogenesis through activation of NF-kappaB pathway.
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Synonyms
RAP2B, member of RAS oncogene family, Ras-related protein Rap-2b, Ras Family Small GTP Binding Protein RAP2B2, Small GTP Binding Protein.
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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 MGSMREYKVV VLGSGGVGKS ALTVQFVTGS FIEKYDPTIE DFYRKEIEVD SSPSVLEILD TAGTEQFASM RDLYIKNGQG FILVYSLVNQ QSFQDIKPMR DQIIRVKRYE RVPMILVGNK VDLEGEREVS YGEGKALAEE WSCPFMETSA KNKASVDELF AEIVRQMNYA AQPNGDEGCC SACVIL.
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 :
SIL1 HumanDescription:
SIL1 Human Recombinant
SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.
Product # :
PRO-1187Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 439 amino acids (32-461) and having a molecular mass of 50.0 kDa.SIL1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SIL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SIL1 is localized to endoplasmic reticulum (ER). SIL1 is an N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. SIL1 acts as a nucleotide exchange factor for another unfolded protein response protein. Mutations in SIL1 are linked to Marinesco-Sjogren syndrome.
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Synonyms
SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.
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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
MHQNLKEFAL TNPEKSSTKE TERKETKAEE ELDAEVLEVF HPTHEWQALQ PGQAVPAGSH VRLNLQTGER EAKLQYEDKF RNNLKGKRLD INTNTYTSQD LKSALAKFKE GAEMESSKED KARQAEVKRL FRPIEELKKD FDELNVVIET DMQIMVRLIN KFNSSSSSLE EKIAALFDLE YYVHQMDNAQ DLLSFGGLQV VINGLNSTEP LVKEYAAFVL GAAFSSNPKV QVEAIEGGAL QKLLVILATE QPLTAKKKVL FALCSLLRHF PYAQRQFLKL GGLQVLRTLV QEKGTEVLAV RVVTLLYDLV TEKMFAEEEA ELTQEMSPEK LQQYRQVHLL PGLWEQGWCE ITAHLLALPE HDAREKVLQT LGVLLTTCRD RYRQDPQLGR TLASLQAEYQ VLASLELQDG EDEGYFQELL GSVNSLLKEL RLEHHHHHH.
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 :
CRP HumanDescription:
C-Reactive Protein Human
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Product # :
PRO-557Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human CRP produced in Human plasma having a molecular mass of 114 kDa. It can be used as a marker for inflammation and also used for monitoring and prediction of future events in coronary artery disease.
Source
Human Plasma.
Formulation
The protein solution is in 20mM TRIS buffer pH 8.0 containing 0.28M NaCl, 0.09% NaN3 and 5mM CaCl2.
Purity
Greater than 96.0%.
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically ( up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Human CRP should be stored at 2-8°C. Do not freeze!
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG and HIV/HBV/HCV (PCR).
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 :
FABP3 Human, NativeDescription:
Fatty Acid Binding Protein-3 Human, Native
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
Product # :
PRO-2794Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FABP3 Human produced in Human cardiac muscle tissue having a molecular mass of 15kDa and is purified by proprietary chromatographic technique.
Source
Human heart tissue.
Formulation
FABP3 was lyophilized from 10mM Tris-HCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fatty Acid Binding Protein-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP3 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 FABP3 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
FABP3 is abundantly expressed in cardiac and skeletal muscle tissues, where it serves as a crucial mediator in the cellular handling of fatty acids. By facilitating the uptake, transport, and utilization of fatty acids, FABP3 ensures a steady supply of energy, making it indispensable for the high-energy-demanding heart and skeletal muscles. Beyond its role in energy metabolism, FABP3 has been implicated in diverse cellular processes, including inflammation, oxidative stress response, and cellular differentiation.
Molecular Insights:
At the molecular level, FABP3 exhibits a remarkable affinity for long-chain fatty acids. Its unique binding properties enable it to shuttle fatty acids to specific cellular compartments, such as mitochondria, for β-oxidation. Additionally, FABP3 is intricately involved in the regulation of gene expression, modulating the activity of various transcription factors and signaling pathways. Understanding these molecular intricacies is key to deciphering FABP3's diverse functions.
Physiological Significance:
In cardiac muscle, FABP3 plays a crucial role in myocardial energy metabolism. During periods of increased energy demand, such as cardiac stress or exercise, FABP3 ensures a rapid supply of fatty acids for ATP production. Its absence or dysfunction has been associated with impaired cardiac function and increased susceptibility to ischemic injury. In skeletal muscles, FABP3 contributes to the utilization of fatty acids as an energy source during sustained physical activity.
Implications in Disease:
Research indicates that alterations in FABP3 expression and function are linked to several pathological conditions. In cardiovascular diseases, FABP3 has emerged as a potential biomarker for myocardial infarction, reflecting myocardial damage. Moreover, studies have highlighted its involvement in insulin resistance, diabetes, and metabolic syndrome, emphasizing its significance in metabolic disorders.
Therapeutic Prospects:
The unique properties of FABP3 have garnered attention in drug development. Researchers are exploring FABP3-targeted therapies for cardiovascular diseases and metabolic disorders. Modulating FABP3 activity presents a promising avenue for managing conditions characterized by dysregulated fatty acid metabolism and oxidative stress.
Conclusion:
FABP3, the unassuming intracellular fatty acid chaperone, plays a central role in human physiology and disease. Its intricate involvement in energy metabolism, cellular signaling, and disease pathogenesis underscores its significance as a research subject. As our understanding of FABP3 deepens, it opens doors to innovative diagnostic approaches and therapeutic interventions, potentially impacting millions of lives worldwide.
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 :
CEACAM3 Human, Sf9Description:
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3 Human Recombinant, Sf9
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, Carcinoembryonic Antigen CGM1, CD66d Antigen , CD66D, CGM1, Carcinoembryonic Antigen Gene Family Member 1, Nonspecific Cross-Reacting Antigen, W264, W282, CEA, CEACAM3.
Product # :
PRO-2443Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEACAM3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 130 amino acids (35-155a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CEACAM3 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CEACAM3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, also known as CEACAM3, is a member of the immunoglobulin super family. The genes in this family encode cell adhesion proteins, which are expressed at higher levels in tumorous tissues rather than in normal tissues. CEACAM3 plays a significant part in the clearance of pathogens through the innate immune system. In addition, CEACAM3 is accountable for RAC1 stimulation in the course of pathogen phagocytosis.
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Synonyms
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, Carcinoembryonic Antigen CGM1, CD66d Antigen , CD66D, CGM1, Carcinoembryonic Antigen Gene Family Member 1, Nonspecific Cross-Reacting Antigen, W264, W282, CEA, CEACAM3.
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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
ADPKLTIESM PLSVAEGKEV LLLVHNLPQH LFGYSWYKGE RVDGNSLIVG YVIGTQQATP GAAYSGRETI YTNASLLIQN VTQNDIGFYT LQVIKSDLVN EEATGQFHVY QENAPGLPVG AVAGHHHHHH.
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 :
TXN1, HisDescription:
Thioredoxin Recombinant, His Tag
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
Product # :
PRO-784Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TRX His Tag protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >70 A650/cm/min/mg, detected by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
More Info
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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in
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Synonyms
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
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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
MHHHHHHMGS DKIIHLTDDS FDTDVLKADG AILVDFWAEW CGPCKMIAPI LDEIADEYQG KLTVAKLNID QNPGTAPKYG IRGIPTLLLF KNGEVAATKV GALSKGQLKE FLDANLAGS.
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 :
Der P1Description:
Der P1 Protein Recombinant
Peptidase 1, Major mite fecal allergen Der p 1, Allergen Der p I, Der p 1, DERP1, Der-P1.
Product # :
ALR-003Price :
Quantity :
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Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the Dermatophagoides pteronyssinus Dust Mite Der P1 protein (a.a. 20-320) and fused to a 6 His Tag at C-terminus, having a total Mw of 34.5kDa, pI 5.6.
Source
Escherichia Coli.
Formulation
60mM NaCl and 50mM Tris-HCl pH 8.0.
Purity
Protein is >95% pure as determined by 10% SDS-PAGE (coomassie staining).
More Info
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Introduction
DERP1 is a thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues. DERP1 is a C1 peptidase family member. DERP1 has extensive endopeptidase specificity. DERP1 is N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites. DERP1 causes an allergic reaction in humans. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. DERP1 binds to IgE in 80% of patients with house dust allergy.
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Synonyms
Peptidase 1, Major mite fecal allergen Der p 1, Allergen Der p I, Der p 1, DERP1, Der-P1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Der-P1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MSIKTFEEYKKAFNKSYATFEDEEAARKNFLESVKYVQSNGGAINHLSDLSLDEFKNRFLMSAEAFEHLKTQFDLNAETNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSAWAFSGVAATESAYLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQRFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLMMIEEYPYVVILHHHHHH.
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Purification Method
Purified by proprietary chromatographic technique.
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 :
Avidin ProteinDescription:
Avidin
Avidin, AVD, AVID.
Product # :
PRO-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- biological activity
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Description
Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).
Source
Hen's egg white.
Biological Activity
15.0 units/mg protein, 1 unit binds 1µg biotin.
More Info
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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
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Synonyms
Avidin, AVD, AVID.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin 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 Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.
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 :
SPA-Cys LongDescription:
Staphylococcal Protein-A Cys Long Form Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1924Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
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Description
SPA-Cys long Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 423 amino acids and having a molecular mass of 46.7kDa containing little or no carbohydrate.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AQHDEAQQNA FYQVLNMPNL NADQRNGFIQ SLKDDPSQSA NVLGEAQKLN DSQAPKADAQ QNNFNKDQQS AFYEILNMPN LNEAQRNGFI QSLKDDPSQS TNVLGEAKKL NESQAPKADN NFNKEQQNAF YEILNMPNLN EEQRNGFIQS LKDDPSQSAN LLSEAKKLNE SQAPKADNKF NKEQQNAFYE ILHLPNLNEE QRNGFIQSLK DDPSQSANLL AEAKKLNDAQ APKADNKFNK EQQNAFYEIL HLPNLTEEQR NGFIQSLKDD PSVSKEILAE AKKLNDAQAP KEEDNKKPGK EDGNKPGKED GNKPGKEDNK KPGKEDGNKP GKEDNNKPGK EDGNKPGKED NNKPGKEDGN KPGKEDGNKP GKEDGNGVHV VKPGDTVNDI AKANGTTADK IAADNKLADK NMIKPGQELV VDC
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 :
SDC2 HumanDescription:
Syndecan-2 Human Recombinant
Syndecan 2, Heparan Sulfate Proteoglycan 1 Cell Surface-Associated, Heparan Sulfate Proteoglycan Core Protein, Syndecan Proteoglycan 2, Fibroglycan, HSPG1, SYND2, HSPG, Cell Surface-Associated Heparan Sulfate Proteoglycan 1, CD362 Antigen, Syndecan-2, CD362, SDC2.
Product # :
PRO-2449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SDC2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 135 amino acids (19-144a.a.) and having a molecular mass of 15kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDC2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SDC2 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.
More Info
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Introduction
Syndecan 2 (SDC2) is a conserved family of heparan- and chondroitin-sulfate carrying transmembrane protein. Syndecan 2 is a cell membrane proteoglycan which modulates the activity and dynamics of some growth factor receptors and integrins. SDC2 is expressed in HSCs (hepatic stellate cells), a key cell type involved in matrix deposition in liver fibrotic disorders. SDC2 is implicated in the formation of specialized membrane domains and serves as a direct link between the extracellular environment and the organization of the cortical cytoplasm.
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Synonyms
Syndecan 2, Heparan Sulfate Proteoglycan 1 Cell Surface-Associated, Heparan Sulfate Proteoglycan Core Protein, Syndecan Proteoglycan 2, Fibroglycan, HSPG1, SYND2, HSPG, Cell Surface-Associated Heparan Sulfate Proteoglycan 1, CD362 Antigen, Syndecan-2, CD362, SDC2.
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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
ADPESRAELT SDKDMYLDNS SIEEASGVYP IDDDDYASAS GSGADEDVES PELTTSRPLP KILLTSAAPK VETTTLNIQN KIPAQTKSPE ETDKEKVHLS DSERKMDPAE EDTNVYTEKH SDSLFKRTEH HHHHH.
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.