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1000 results found for “Peroxiredoxin”
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Name :
CXCL1 HumanDescription:
GRO-Alpha Human Recombinant (CXCL1)
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Product # :
CHM-329Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.
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 peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 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-Ser-Val-Ala-Thr.
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Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.
What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 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.
- View Data Sheet
Name :
CXCL3 HumanDescription:
GRO-Gamma Human Recombinant (CXCL3)
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
Product # :
CHM-310Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
GRO-Gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7902 Dalton. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 CXCL3 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-Ser-Val-Val-Thr.
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Background
What is the molecular weight/Mw of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein has a total Mw of 7.9kDa.
What is the source or expression system of CXCL3 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL3 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.
What applications can CXCL3 HUMAN Protein be used in?
CXCL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 HUMAN Protein?
The endotoxin level is minimal, CXCL3 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 :
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 :
PTPMT1 HumanDescription:
Protein Tyrosine Phosphatase, Mitochondrial 1 Human Recombinant
Protein-tyrosine phosphatase mitochondrial 1, PTEN-like phosphatase, Phosphoinositide lipid phosphatase, PTPMT1, MOSP, PLIP, DUSP23, PNAS-129.
Product # :
ENZ-225Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTPMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (28-201) and having a molecular mass of 22.6kDa.PTPMT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PTPMT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein tyrosine phosphatase mitochondrial 1 (PTPMT1) is a broadly expressed PTP membrane protein with high expression levels in pancreatic beta cells. The PTPMT1 protein is completely restricted to the matrix face of the inner membrane of the mitochondrion. PTPMT1 is responsible for dephosphorylating mitochondrial proteins and thus has a major role in the production of ATP. PTPMT1 exhibits a specific preference for the lipid signaling molecule phosphatidylinositol 5-phosphate as substrate.
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Synonyms
Protein-tyrosine phosphatase mitochondrial 1, PTEN-like phosphatase, Phosphoinositide lipid phosphatase, PTPMT1, MOSP, PLIP, DUSP23, PNAS-129.
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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 MGSHMKVPGR AHRDWYHRID PTVLLGALPL RSLTRQLVQD ENVRGVITMN EEYETRFLCN SSQEWKRLGV EQLRLSTVDM TGIPTLDNLQ KGVQFALKYQ SLGQCVYVHC KAGRSRSATM VAAYLIQVHK WSPEEAVRAI AKIRSYIHIR PGQLDVLKEF HKQITARATK DGTFVISKT.
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 :
VAMP8 HumanDescription:
Endobrevin Human Recombinant
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Product # :
PRO-660Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.
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Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.
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 :
CNDP2 HumanDescription:
CNDP Dipeptidase 2 Human Recombinant
Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.
Product # :
ENZ-681Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CNDP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 498 amino acids (1-475) and having a molecular mass of 55.3 kDa. CNDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CNDP2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.
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Synonyms
Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.
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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 MGSMAALTTL FKYIDENQDR YIKKLAKWVA IQSVSAWPEK RGEIRRMMEV AAADVKQLGG SVELVDIGKQ KLPDGSEIPL PPILLGRLGS DPQKKTVCIY GHLDVQPAAL EDGWDSEPFT LVERDGKLYG RGSTDDKGPV AGWINALEAY QKTGQEIPVN VRFCLEGMEE SGSEGLDELI FARKDTFFKD VDYVCISDNY WLGKKKPCIT YGLRGICYFF IEVECSNKDL HSGVYGGSVH EAMTDLILLM GSLVDKRGNI LIPGINEAVA AVTEEEHKLY DDIDFDIEEF AKDVGAQILL HSHKKDILMH RWRYPSLSLH GIEGAFSGSG AKTVIPRKVV GKFSIRLVPN MTPEVVGEQV TSYLTKKFAE LRSPNEFKVY MGHGGKPWVS DFSHPHYLAG RRAMKTVFGV EPDLTREGGS IPVTLTFQEA TGKNVMLLPV GSADDGAHSQ NEKLNRYNYI EGTKMLAAYL YEVSQLKD.
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 :
COX4NB HumanDescription:
COX4NB Human Recombinant
COX4 neighbor, COX4AL, Protein FAM158B, NOC4, C16orf2, chromosome 16 open reading frame 2, C16orf4, chromosome 16 open reading frame 4, family with sequence similarity 158-member B.
Product # :
PRO-917Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
COX4NB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-210) and having a molecular mass of 25.9 kDa.The COX4NB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The COX4NB solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
COX4NB is a member of the UPF0172 (NOC4) family and is located on chromosome 16, next to the COX4 gene. The COX4NB is expressed in high levels in the pancreas, moderate levels in the heart, skeletal muscle, and placenta and low levels in the liver, lung, kidney and brain.
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Synonyms
COX4 neighbor, COX4AL, Protein FAM158B, NOC4, C16orf2, chromosome 16 open reading frame 2, C16orf4, chromosome 16 open reading frame 4, family with sequence similarity
158-member B. -
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 MPGVKLTTQA YCKMVLHGAK YPHCAVNGLL VAEKQKPRKE HLPLGGPGAH HTLFVDCIPL FHGTLALAPM LEVALTLIDS WCKDHSYVIA GYYQANERVK DASPNQVAEK VASRIAEGFS DTALIMVDNT KFTMDCVAPT IHVYEHHENR WRCRDPHHDY CEDWPEAQRI SASLLDSRSY ETLVDFDNHL DDIRNDWTNP EINKAVLHLC
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 :
CPLX1 HumanDescription:
Complexin-1 Human Recombinant
CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.
Product # :
PRO-645Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CPLX1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-134 a.a) and having a molecular mass of 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 90% by SDS-PAGE.
More Info
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Introduction
CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.
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Synonyms
CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.
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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 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.
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 :
YWHAG HumanDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
Product # :
PKA-238Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-247) and having a molecular mass of 28 kDa. YWHAG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAG solution containing 20mM Tris 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
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Synonyms
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
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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
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN.
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 :
Luciferase FireflyDescription:
Luciferin 4-Monooxygenase Firefly Recombinant
Luciferase-like monooxygenase, LUC, EC 1.13.12.7.
Product # :
ENZ-553Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-550 a.a.) and having a molecular mass of 62.9kDa.Luciferase is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Luciferase protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.
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Synonyms
Luciferase-like monooxygenase, LUC, EC 1.13.12.7.
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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 MMEDAKNIKK GPAPFYPLED GTAGEQLHKA MKRYALVPGT IAFTDAHIEV DITYAEYFEM SVRLAEAMKR YGLNTNHRIV VCSENSLQFF MPVLGALFIG VAVAPANDIY NERELLNSMG ISQPTVVFVS KKGLQKILNV QKKLPIIQKI IIMDSKTDYQ GFQSMYTFVT SHLPPGFNEY DFVPESFDRD KTIALIMNSS GSTGLPKGVA LPHRTACVRF SHARDPIFGN QIIPDTAILS VVPFHHGFGM FTTLGYLICG FRVVLMYRFE EELFLRSLQD YKIQSALLVP TLFSFFAKST LIDKYDLSNL HEIASGGAPL SKEVGEAVAK RFHLPGIRQG YGLTETTSAI LITPEGDDKP GAVGKVVPFF EAKVVDLDTG KTLGVNQRGE LCVRGPMIMS GYVNNPEATN ALIDKDGWLH SGDIAYWDED EHFFIVDRLK SLIKYKGYQV APAELESILL QHPNIFDAGV AGLPDDDAGE LPAAVVVLEH GKTMTEKEIV DYVASQVTTA KKLRGGVVFV DEVPKGLTGK LDARKIREIL IKAKKGGKIA 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.
- View Data Sheet
Name :
Borrelia Bavariensis DbpADescription:
Borrelia Bavariensis DbpA Recombinant
Decorin binding protein A, dbpA.
Product # :
BOR-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Borrelia Bavariensis DbpA produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 18kDa. Borrelia Bavariensis DbpA is expressed with a 10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Bavariensis DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Borrelia is a part of a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Borreliella bavariensis is one of the pathogens of the Borreliella burgdorferi sensu lato complex which causes Lyme disease. Decorin binding protein A (DbpA), also known as Osp17 or p17 is expressed during the mammalian phase of infection. DbpA is binds the pathogen to host collagen-associated proteoglycan decorin.
-
Synonyms
Decorin binding protein A, dbpA.
-
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.
-
Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative patient samples.
-
Applications
Western blot with Patient sample.
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 :
Tamm HorsfallDescription:
Recombinant Human Tamm Horsfall Glycoprotein
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-1206Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- SDS-PAGE
Description
Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.
Source
HEK293
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
SDS-PAGE
More Info
-
Introduction
Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.
-
Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
-
Solubility
Add deionized water to prepare a working stock solution of approximately 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.
-
Amino Acid Sequence
DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH
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Background
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
What is the molecular weight/Mw of UMOD Protein?
UMOD Protein has a total Mw of 65kDa.
What is the source or expression system of UMOD Protein?
HEK293.
What is the Purity of UMOD Protein?
UMOD Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of UMOD Protein?
The biological functionality of UMOD Protein will be determined in the future.
What is the amino acid sequence of UMOD Protein?
UMOD Protein is composed from 595 amino acids.
What applications can UMOD Protein be used in?
UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for UMOD Protein?
The endotoxin level is minimal, UMOD 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 :
MX1 HumanDescription:
Myxovirus Resistance 1 Human Recombinant
MX Dynamin-Like GTPase 1, Myxoma Resistance Protein 1, IFI-78K, IFI78, MX, Myxovirus (Influenza) Resistance 1,
Product # :
PRO-2091Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
MX1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 685 amino acids (1-662 a.a) and having a molecular mass of 77.9kDa. MX1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MX1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Myxovirus Resistance 1, also known as MX1 is a guanosine triphosphate (GTP)-metabolizing protein which takes part in the cellular antiviral response. MX1 is induced by type I and type II IFN, and also antagonizes the replication process of some different RNA & DNA viruses. In addition, there is a related gene located adjacent to MX1 on chromosome 21, and there are multiple pseudogenes positioned in a cluster on chromosome 4.
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Synonyms
MX Dynamin-Like GTPase 1, Myxoma Resistance Protein 1, IFI-78K, IFI78, MX, Myxovirus (Influenza) Resistance 1,
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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. 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 MGSMVVSEVD IAKADPAAAS HPLLLNGDAT VAQKNPGSVA ENNLCSQYEE KVRPCIDLID SLRALGVEQD LALPAIAVIG DQSSGKSSVL EALSGVALPR GSGIVTRCPL VLKLKKLVNE DKWRGKVSYQ DYEIEISDAS EVEKEINKAQ NAIAGEGMGI SHELITLEIS SRDVPDLTLI DLPGITRVAV GNQPADIGYK IKTLIKKYIQ RQETISLVVV PSNVDIATTE ALSMAQEVDP EGDRTIGILT KPDLVDKGTE DKVVDVVRNL VFHLKKGYMI VKCRGQQEIQ DQLSLSEALQ REKIFFENHP YFRDLLEEGK ATVPCLAEKL TSELITHICK SLPLLENQIK ETHQRITEEL QKYGVDIPED ENEKMFFLID KVNAFNQDIT ALMQGEETVG EEDIRLFTRL RHEFHKWSTI IENNFQEGHK ILSRKIQKFE NQYRGRELPG FVNYRTFETI VKQQIKALEE PAVDMLHTVT DMVRLAFTDV SIKNFEEFFN LHRTAKSKIE DIRAEQEREG EKLIRLHFQM EQIVYCQDQV YRGALQKVRE KELEEEKKKK SWDFGAFQSS SATDSSMEEI FQHLMAYHQE ASKRISSHIP LIIQFFMLQT YGQQLQKAML QLLQDKDTYS WLLKERSDTS DKRKFLKERL ARLTQARRRL AQFPG.
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 :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
More Info
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
UBE2M HumanDescription:
Ubiquitin Conjugating Enzyme E2M Human Recombinant
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
Product # :
ENZ-345Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- More Info
Description
UBE2M Human Recombinant produced E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.5kDa.UBE2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2M solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.
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Synonyms
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
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Physical Appearance
Sterile filtered colorless 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. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIKLFS LKQQKKEEES AGGTKGSSKK ASAAQLRIQK DINELNLPKT CDISFSDPDD LLNFKLVICP DEGFYKSGKF VFSFKVGQGY PHDPPKVKCE TMVYHPNIDL EGNVCLNILR EDWKPVLTIN SIIYGLQYLF LEPNPEDPLN KEAAEVLQNN RRLFEQNVQR SMRGGYIGST YFERCLK
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 :
HDGFL1 HumanDescription:
Hepatoma Derived Growth Factor-Like 1 Human Recombinant
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
Product # :
CYT-850Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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- purity
- More Info
Description
HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.
-
Synonyms
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
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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. 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 MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
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Background
What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.
What is the source or expression system of HDGFL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HDGFL1 HUMAN Protein?
The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of HDGFL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
What applications can HDGFL1 HUMAN Protein be used in?
HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HDGFL1 HUMAN Protein?
The endotoxin level is minimal, HDGFL1 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.
- View Data Sheet
Name :
MOCS2 HumanDescription:
Molybdenum Cofactor Synthesis 2 Human Recombinant
Molybdenum Cofactor Synthesis 2, Molybdopterin Synthase Sulfur Carrier Subunit, Molybdenum Cofactor Biosynthesis Protein E, MPT Synthase Large Subunit, Molybdopterin Synthase Catalytic Subunit, Molybdenum Cofactor Synthesis Protein 2 Large Subunit, Molybdenum Cofactor Synthesis Protein 2 Small Subunit, Molybdenum Cofactor Synthesis Protein 2A, Molybd enum Cofactor Synthesis Protein 2B, Sulfur Carrier Protein MOCS2A, MCBPE, MOCO1, MOCO1-A, MOCO1-B, MOCS2A, MOCS2B, MPTS, EC 2.8.1.12.
Product # :
PRO-1281Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
MOCS2 Human Recombinant produced in E. coli is a single polypeptide chain containing 224 amino acids (1-188) and having a molecular mass of 25.0 kDa.MOCS2 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MOCS2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Molybdenum Cofactor Synthesis 2 (MOCS2) is a heterotetrameric synthase comprised of 2 small (MOCS2A) and 2 large (MOCS2B) subunits. Both the large and small subunits of molybdopterin synthase are encoded from the MOCS2 gene by overlapping open reading frames. MOCS2 operates in the second step of the molybdenum cofactor or molybdopterin (MPT) synthesis. MOCS2 catalyzes the formation of MPT from precursor Z by incorporating a dithiolene functional group.
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Synonyms
Molybdenum Cofactor Synthesis 2, Molybdopterin Synthase Sulfur Carrier Subunit, Molybdenum Cofactor Biosynthesis Protein E, MPT Synthase Large Subunit, Molybdopterin Synthase Catalytic Subunit, Molybdenum Cofactor Synthesis Protein 2 Large Subunit, Molybdenum Cofactor Synthesis Protein 2 Small Subunit, Molybdenum Cofactor Synthesis Protein 2A, Molybd enum Cofactor Synthesis Protein 2B, Sulfur Carrier Protein MOCS2A, MCBPE, MOCO1, MOCO1-A, MOCO1-B, MOCS2A, MOCS2B, MPTS, EC 2.8.1.12.
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Physical Appearance
Sterile Filtered colorless 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. 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 KDRWGSMSSL EISSSCFSLE TKLPLSPPLV EDSAFEPSRK DMDEVEEKSK DVINFTAEKL SVDEVSQLVI SPLCGAISLF VGTTRNNFEG KKVISLEYEA YLPMAENEVR KICSDIRQKW PVKHIAVFHR LGLVPVSEAS IIIAVSSAHR AASLEAVSYA IDTLKAKVPI WKKEIYEESS TWKGNKECFW ASNS
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 :
AHCY Human, Sf9Description:
Adenosylhomocysteinase Human Recombinant, Sf9
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
Product # :
ENZ-1034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- More Info
Description
AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AHCY protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
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Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
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Physical Appearance
Sterile Filtered colorless 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. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH 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.
- View Data Sheet
Name :
AMELX HumanDescription:
Amelogenin, X-Linked Human Recombinant
Amelogenin X isoform, AMELX, AMG, AMGX, AI1E, AIH1, ALGN, AMGL.
Product # :
PRO-1324Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
AMELX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (17-191 a.a) and having a molecular mass of 22kDa.AMELX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AMELX protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Amelogenin, X-Linked (AMELX) belongs to the amelogenin family of extracellular matrix proteins. Amelogenins have a role biomineralization during tooth enamel development. AMELX gene mutations cause X-linked amelogenesis imperfecta. AMELX regulates the formation of crystallites during the secretory stage of tooth enamel development. AMELX is transiently but amply expressed by ameloblasts during tooth development. Amelogenin is the principal protein in developing dental enamel.
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Synonyms
Amelogenin X isoform, AMELX, AMG, AMGX, AI1E, AIH1, ALGN, AMGL.
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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 MGSMPLPPHP GHPGYINFSY EVLTPLKWYQ SIRPPYPSYG YEPMGGWLHH QIIPVLSQQH PPTHTLQPHH HIPVVPAQQP VIPQQPMMPV PGQHSMTPIQ HHQPNLPPPA QQPYQPQPVQ PQPHQPMQPQ PPVHPMQPLP PQPPLPPMFP MQPLPPMLPD LTLEAWPSTD KTKREEVD.
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 :
SIKE1 HumanDescription:
Suppressor Of IKBKE 1 Human Recombinant
Suppressor Of IKBKE 1, SIKE, Suppressor Of IKK Epsilon, Suppressor Of IKK-Epsilon.
Product # :
PRO-1913Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
SIKE1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a) and having a molecular mass of 26.1kDa.SIKE1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIKE1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Suppressor of IKBKE 1 also known as SIKE1 belongs to the SIKE family. SIKE interacts with IKK-epsilon and TBK1 and function as a suppressor of TLR3. In addition, SIKE1 perform by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 andDDX58/RIG-I. SIKE1 does not inhibit NF-kappa-B activation pathways.
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Synonyms
Suppressor Of IKBKE 1, SIKE, Suppressor Of IKK Epsilon, Suppressor Of IKK-Epsilon.
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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 MGSMSCTIEK ILTDAKTLLE RLREHDAAAE SLVDQSAALH RRVAAMREAG TALPDQYQED ASDMKDMSKY KPHILLSQEN TQIRDLQQEN RELWISLEEH QDALELIMSK YRKQMLQLMV AKKAVDAEPV LKAHQSHSAE IESQIDRICE MGEVMRKAVQ VDDDQFCKIQ EKLAQLELEN KELRELLSIS SESLQARKEN SMDTASQAIK
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 :
BAFFR Human, HEKDescription:
BAFF (BLyS) Receptor Human Recombinant, HEK
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
Product # :
CYT-1224Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- biological activity
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Description
BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.
More Info
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Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
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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
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.
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Background
B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.
Structural Architecture of BAFF Receptor Protein:
BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.
Physiological Significance in B-Cell Biology:
BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.
Regulation of Immune Responses:
BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.
BAFF Receptor as a Therapeutic Target:
The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.
BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.
What is the molecular weight/Mw of BAFF-R Protein?
BAFF-R Protein has a total Mw of 34.4kDa.
What is the source or expression system of BAFF-R Protein?
HEK293 Cells.
What is the Purity of BAFF-R Protein?
BAFF-R Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BAFF-R Protein?
The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.
What is the amino acid sequence of BAFF-R Protein?
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.
What applications can BAFF-R Protein be used in?
BAFF-R Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BAFF-R Protein?
The endotoxin level is minimal, BAFF-R 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 :
ENTPD3 Human, sf9Description:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
Product # :
ENZ-958Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ENTPD3 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 451 amino acids (44-485a.a) and having a molecular mass of 50.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ENTPD3 protein solution (0.5mg/ml) containing 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
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
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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
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.
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 :
OstreolysinDescription:
Ostreolysin Pleurotus Ostreatus Recombinant
Product # :
PRO-2600Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ostreolysin protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines.
More Info
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Introduction
Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pleurotus Ostreatus Ostreolysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted Ostreolysin should be stored at 4°C below -18°C. 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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Solubility
It is recommended to reconstitute the lyophilized Ostreolysin in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The N-terminal amino sequence is Ala-Tyr-Ala-Gln-Trp-Val.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.
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 :
PRCP HumanDescription:
Prolylcarboxypeptidase Human Recombinant
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
Product # :
ENZ-1178Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa. PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PRCP solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3,000 pmol/min/μg, and is defined as the amount of enzyme that converts 1pmole of Z-ProAla-OH/min. at pH-4 at 25˚C.
More Info
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Introduction
PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.
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Synonyms
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
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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
LRPALRALGS LHLPTNPTSL PAVAKNYSVL YFQQKVDHFG FNTVKTFNQR YLVADKYWKK NGGSILFYTG NEGDIIWFCN NTGFMWDVAE ELKAMLVFAE HRYYGESLPF GDNSFKDSRH LNFLTSEQAL ADFAELIKHL KRTIPGAENQ PVIAIGGSYG GMLAAWFRMK YPHMVVGALA ASAPIWQFED LVPCGVFMKI VTTDFRKSGP HCSESIHRSW DAINRLSNTG SGLQWLTGALHLCSPLTSQD IQHLKDWISE TWVNLAMVDY PYASNFLQPL PAWPIKVVCQ YLKNPNVSDS LLLQNIFQAL NVYYNYSGQV KCLNISETAT SSLGTLGWSY QACTEVVMPF CTNGVDDMFE PHSWNLKELS DDCFQQWGVR PRPSWITTMY GGKNISSHTN IVFSNGELDP WSGGGVTKDI TDTLVAVTIS EGAHHLDLRT KNALDPMSVL LARSLEVRHM KNWIRDFYDS AGKQ HHHHHH
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.