Search results
1000 results found for “CEBP”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
CPA4 HumanDescription:
Carboxypeptidase A4 Human Recombinant
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
Product # :
ENZ-942Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CPA4 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
-
Introduction
Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.
-
Synonyms
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
-
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
GQEKFFGDQV LRINVRNGDE ISKLSQLVNS NNLKLNFWKS PSSFNRPVDV LVPSVSLQAF KSFLRSQGLE YAVTIEDLQA LLDNEDDEMQ HNEGQERSSN NFNYGAYHSL EAIYHEMDNI AADFPDLARR VKIGHSFENR PMYVLKFSTG KGVRRPAVWL NAGIHSREWI SQATAIWTAR KIVSDYQRDP AITSILEKMD IFLLPVANPD GYVYTQTQNR LWRKTRSRNP GSSCIGADPN RNWNASFAGK GASDNPCSEV YHGPHANSEV EVKSVVDFIQ KHGNFKGFID LHSYSQLLMY PYGYSVKKAP DAEELDKVAR LAAKALASVS GTEYQVGPTC TTVYPASGSS IDWAYDNGIK FAFTFELRDT GTYGFLLPAN QIIPTAEETW LGLKTIMEHV RDNLYLEHHH HHH.
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 :
CRYBB1 HumanDescription:
Crystallin Beta B1 Human Recombinant
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
Product # :
HSP-033Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CRYBB1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (1-252 a.a.) and having a molecular mass of 29.1 kDa. The CRYBB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYBB1 solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Crystallins are the main structural proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into 3 fprotein families, α, β, & γ families. Because lens central fiber cells lose their nuclei during development, these crystallins are prepared and then retained throughout life, making them extremely stable proteins. CRYBB1 is a beta basic group member and undergoes extensive cleavage at its N-terminal extension during lens maturation.
-
Synonyms
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
-
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
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PKRSHHHHHH.
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 :
CXCL13 MouseDescription:
BCA-1/BLC Mouse Recombinant (CXCL13)
C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.
Product # :
CHM-030Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.More Info
-
Introduction
BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.
-
Synonyms
C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.
-
Background
What is the molecular weight/Mw of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein has a total Mw of 10kDa.
What is the source or expression system of CXCL13 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL13 MOUSE Protein?
The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.
What is the amino acid sequence of CXCL13 MOUSE Protein?
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.
What applications can CXCL13 MOUSE Protein be used in?
CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL13 MOUSE Protein?
The endotoxin level is minimal, CXCL13 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.
- View Data Sheet
Name :
IL18BP HumanDescription:
Interleukin-18 Binding Protein Human Recombinant
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.
Product # :
CYT-728Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IL18BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (31-194 a.a) and having a molecular mass of 20kDa. IL18BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL18BP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.
-
Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQG.
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 :
CBR3 HumanDescription:
Carbonyl Reductase-3 Human Recombinant
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
Product # :
ENZ-428Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human CBR3 fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-277 a.a) and having a molecular mass of 33kDa. CBR3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CBR3 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
-
Introduction
CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.
-
Synonyms
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
-
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 MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW.
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 Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human 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
Human 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 activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Human 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 Human pegylated leptin antagonist and filter sterilization Human 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.
-
Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant 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.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant 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.
-
Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. 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.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GM-CSF Human, PichiaDescription:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Product # :
CYT-324Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.
Purity
Greater than 97.0% as determined by1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.More Info
-
Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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.
-
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
-
Background
What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.
What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
Pichia Pastoris.
What is the Purity of GM-CSF HUMAN, PICHIA Protein?
GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.
What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
What applications can GM-CSF HUMAN, PICHIA Protein be used in?
GM-CSF HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF HUMAN, PICHIA Protein?
The endotoxin level is minimal, GM-CSF HUMAN, PICHIA 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 :
SERPINB4 HumanDescription:
Serpin Peptidase Inhibitor, Clade B Member 4 Human Recombinant
SERPINB4, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member, Squamous Cell Carcinoma, Antigen, SCCA2, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member, Peptidase Inhibitor, LEUPIN, SCCA, PI11, Protease Inhibitor (Leucine-Serpin) Squamous Cell Carcinoma Antigen, SCCA2/SCCA1 Fusion Protein, Serpin B4, SCCA1 PI-11.
Product # :
PRO-2208Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SERPINB4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-390 a.a) and having a molecular mass of 47.2kDa.SERPINB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERPINB4 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Serpin Peptidase Inhibitor, Clade B Member 4, also known as SERPINB4 is a member of the serpin family. SERPINB4 acts as a protease inhibitor to modulate the host immune response against tumor cells. Among the diseases associated with SERPINB4 are: inverted papilloma as well as burns.
-
Synonyms
SERPINB4, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member, Squamous Cell Carcinoma, Antigen, SCCA2, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member, Peptidase Inhibitor, LEUPIN, SCCA, PI11, Protease Inhibitor (Leucine-Serpin) Squamous Cell Carcinoma Antigen, SCCA2/SCCA1 Fusion Protein, Serpin B4, SCCA1 PI-11.
-
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 MGSMEDLCVA NTLFALNLFK HLAKASPTQN LFLSPWSISS TMAMVYMGSR GSTEDQMAKV LQFNEVGANA VTPMTPENFT SCGFMQQIQK GSYPDAILQA QAADKIHSSF RSLSSAINAS TGNYLLESVN KLFGEKSASF REEYIRLCQK YYSSEPQAVD FLECAEEARK KINSWVKTQT KGKIPNLLPE GSVDGDTRMV LVNAVYFKGK WKTPFEKKLN GLYPFRVNSA QRTPVQMMYL REKLNIGYIE DLKAQILELP YAGDVSMFLL LPDEIADVST GLELLESEIT YDKLNKWTSK DKMAEDEVEV YIPQFKLEEH YELRSILRSM GMEDAFNKGR ANFSGMSERN DLFLSEVFHQ AMVDVNEEGT EAAAGTGGVM TGRTGHGGPQ FVADHPFLFL IMHKITNCIL FFGRFSSP.
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 :
SNRPB2 HumanDescription:
Small Nuclear Ribonucleoprotein Polypeptide B Human Recombinant
Small nuclear ribonucleoprotein polypeptide B2, Msl1, U2 snRNP B'', U2 small nuclear ribonucleoprotein B'', MGC24807, MGC45309.
Product # :
PRO-217Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNRPB2 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 245 amino acids (1-225a.a.) and having a molecular mass of 27.6kDa. The SNRPB2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNRPB2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
SNRPB2 is a member of the RRM U1 A/B family. SNRPB2 links with stem loop IV of U2 small nuclear ribonucleoprotein (U2 snRNP) in the presence of snRNP-A. SNRPB2 has a part in pre-mRNA splicing. Autoantibodies from patients with systemic lupus erythematosus often identify epitopes on the encoded protein. A pair of transcript variants encoding the same protein were identified for this gene.
-
Synonyms
Small nuclear ribonucleoprotein polypeptide B2, Msl1, U2 snRNP B'', U2 small nuclear ribonucleoprotein B'', MGC24807, MGC45309.
-
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 MDIRPNHTIY INNMNDKIKK EELKRSLYAL FSQFGHVVDI VALKTMKMRG QAFVIFKELG SSTNALRQLQ GFPFYGKPMR IQYAKTDSDI ISKMRGTFAD KEKKKEKKKA KTVEQTATTT NKKPGQGTPN SANTQGNSTP NPQVPDYPPN YILFLNNLPE ETNEMMLSML FNQFPGFKEV RLVPGRHDIA FVEFENDGQA GAARDALQGF KITPSHAMKI TYAKK
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 :
EIF3J HumanDescription:
Eukaryotic Translation Initiation Factor 3J Human Recombinant
Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.
Product # :
PRO-970Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EIF3J Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (70-258) and having a molecular mass of 24kDa (Molecular weight on SDS-PAGE will appear higher).EIF3J is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF3J solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Eukaryotic translation initiation factor 3 subunit J (EIF3J) is a member of the EIF-3 subunit J family. EIF3 has a crucial role in binding of initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to produce the 40S initiation complex. EIF3J binds to the aminoacyl (A) site and mRNA access channel of the 40S subunit, setting EIF3J directly in the ribosomal decoding center. In addition, EIF3J interacts with eIF1A and reduces 40S subunit affinity for mRNA. An elevated affinity for mRNA is restored upon enlistment of initiator tRNA, despite the fact EIF3J remains in the mRNA-binding cleft in the presence of tRNA.
-
Synonyms
Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.
-
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 MKISEKKKIA EKIKEKERQQ KKRQEEIKKR LEEPEEPKVL TPEEQLADKL RLKKLQEESD LELAKETFGV NNAVYGIDAM NPSSRDDFTE FGKLLKDKIT QYEKSLYYAS FLEVLVRDVC ISLEIDDLKK ITNSLTVLCS EKQKQEKQSK AKKKKKGVVP GGGLKATMKD DLADYGGYDG GYVQDYEDFM.
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 :
TBPL1 HumanDescription:
TBP-Like 1 Human Recombinant
TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.
Product # :
PRO-736Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TBPL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (1-186 a.a) and having a molecular mass of 23.3kDa.TBPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TBPL1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
TBP-Like 1 (TBPL1) is a member of the TBP family. The TATA box-binding protein (TBP) is an indispensable component of the basal transcriptional machinery. TBPL1 is crucial for spermiogenesis and supposed to be significant in expression of developmentally regulated genes.
-
Synonyms
TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.
-
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 MGSMDADSDV ALDILITNVV CVFRTRCHLN LRKIALEGAN VIYKRDVGKV LMKLRKPRIT ATIWSSGKII CTGATSEEEA KFGARRLARS LQKLGFQVIF TDFKVVNVLA VCNMPFEIRL PEFTKNNRPH ASYEPELHPA VCYRIKSLRA TLQIFSTGSI TVTGPNVKAV ATAVEQIYPF VFESRKEIL.
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 :
TPRKB HumanDescription:
TP53RK Binding Protein Human Recombinant
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
Product # :
PRO-1185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.
-
Synonyms
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
-
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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL
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 :
CNDP1 MouseDescription:
CNDP Dipeptidase 1 Mouse Recombinant
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 1.
Product # :
ENZ-977Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNDP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (1-492 a.a.) and having a molecular mass of 56.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
-
Synonyms
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 1.
-
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
MFSSAHSGLL EKLFHYIDLH QDEFVQTLKE WVAIESDSVQ PVPRLRQKLF QMMALAADKL RNLGAGVESI DLGSQQMPDG QSLPIPPILL AELGSDPEKP TVCFYGHLDV QPAQKDDGWL TDPYTLTEVD GKLYGRGATD NKGPVLAWIN AVSTFRALQQ DLPVNIKLIL EGMEEAGSIA LEELVMREKD HFFSSVDYIV ISDNLWLSQR KPALTYGTRG NCYFTVEVKC RDQDFHSGTF GGILNEPMAD LVALLGSLVD SSGHILIPGI YDQMAPITEG EKTMYKNIDM DLEEYQNINQ VEKFLFDTKE ELLMHLWRYP SLSIHGIEGA FDEPGTKTVI PGRVLGKFSI RLVPTMSPSV VEKQVTQHLE AVFSKRNSFN KMAVSMVLGL HPWTANVNDT QYLAAQRTIK TVFGVNPDMI RDGSTIPIAK IFQAITQKSV MMLPLGAVDD GEHSQNEKIN RWNYIQGSKL FAAFFLELSK QHSGHQMPSS VYLEHHHHHH.
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 :
LACTB E.coliDescription:
Beta Lactamase E.coli Recombinant
b-Lactamase, EC 3.5.2.6, TEM-1.
Product # :
ENZ-351Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Recombinant E.coli Beta-Lactamase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of approximately 28.9 kDa. Beta Lactamase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated solution in 100mM Tris, pH7.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
One unit will hydrolyze 1.0 μmole of benzyl penicillin at pH 7.0 at 25°C, in presence of EDTA.
More Info
-
Introduction
Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.
-
Synonyms
b-Lactamase, EC 3.5.2.6, TEM-1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Beta Lactamase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Beta Lactamase Recombinant 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.
-
Solubility
It is recommended to reconstitute the lyophilized Beta Lactamase in sterile 18MΩ-cm H2O at a concentration of 100 µg/ml, which can then be further diluted to other aqueous solutions. The Beta Lactamase should be used in pH 7.0- 8.0 and in temperature not higher then 45°c.
-
Amino Acid Sequence
MHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW.
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 :
CST3 Human, PichiaDescription:
Cystatin C Human Recombinant, Pichia
Product # :
PRO-2743Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human Cystatin C is having a molecular mass of approximately 13kDa.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from 20mM NH4HCO3.
Purity
Greater than 96.0%.
More Info
-
Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and subsequently, the atherosclerosis and abdominal aortic aneurysm.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Human CST3 although stable at 4°C for 1 week, should be stored at -20°C.
-
Solubility
It is recommended to reconstitute the lyophilized CST3 Human in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous 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 :
EBV p18Description:
Epstein-Barr Virus (HHV-4) p18 Recombinant
Product # :
EBV-273Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant mosaic protein contains the HHV-4 p18 regions, 1-119 amino acids and fused to a GST-Tag at C-terminus.
Formulation
Containing 25mM Tris-HCl pH 8.0, 1.5M urea and 50% glycerol.
Purity
EBV-p18 protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
-
Introduction
The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virusof the herpes family(which includes Herpes simplex virusand Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expressionwhich can be broadly categorized as being lytic cycle or latent cycle. The lytic cycleor productive infection results in staged expression of a host of viral proteinswith the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cellas EBV virions are produced by budding from the infected cell. The latent cycle(lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen(EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins(LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs(EBERs).
-
Stability
EBV p18 M although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
EBV-p18 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HHV-4 (EBV) with minimal specificity problems.
-
Specificity
Immunoreactive with sera of EBV-infected individuals.
-
Purification Method
EBV-p18 was 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 :
CST1 HumanDescription:
Cystatin SN Human Recombinant
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
Product # :
PRO-1006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (21-141 a.a.) and having a molecular mass of 16.9kDa. CST1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CST1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Cystatin-SN (CST1) belongs to the type 2 salivary cystatin family found in a variety of fluids and secretions, including plasma, tears, and saliva. The cystatin superfamily includes proteins which contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, whereas others have lost or possibly never developed this inhibitory activity. CST1 is up-regulated in cancerous lesions of gastric cancer tissues compared to noncancerous regions, in addition clinicopathological analysis revealed a significant correlation between high expression of CST1.
-
Synonyms
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
-
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 MGSMWSPKEE DRIIPGGIYN ADLNDEWVQR ALHFAISEYN KATKDDYYRR PLRVLRARQQ TVGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WENRRSLVKS RCQES.
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 :
MIP 1b RatDescription:
Macrophage Inflammatory Protein-1 beta Rat Recombinant (CCL4)
C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.
Product # :
CHM-003Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MIP-1b Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids and having a molecular mass of 7.8 kDa. The MIP-1b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 30% Acetonitrile and 0.1% TFA.
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 monocytes using a concentration range of 0.01-1.0 µg/ml.More Info
-
Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1? and MIP-1? 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-? from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
-
Synonyms
C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CCL4 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.
-
Solubility
It is recommended to reconstitute the lyophilized Mouse MIP-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.
-
Background
What is the molecular weight/Mw of MIP 1B RAT Protein?
MIP 1B RAT Protein has a total Mw of 7.8kDa.
What is the source or expression system of MIP 1B RAT Protein?
Escherichia Coli.
What is the Purity of MIP 1B RAT Protein?
MIP 1B RAT Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1B RAT Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.01-1.0 µg/ml.
What is the amino acid sequence of MIP 1B RAT Protein?
APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.
What applications can MIP 1B RAT Protein be used in?
MIP 1B RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1B RAT Protein?
The endotoxin level is minimal, MIP 1B RAT 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 :
SEP15 HumanDescription:
15 KDa Selenoprotein Human Recombinant
15 KDa Selenoprotein, SEP15.
Product # :
PRO-1468Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SEP15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (29-165 a.a) and having a molecular mass of 17.7kDa.SEP15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEP15 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
15 KDa Selenoprotein (SEP15) is a protein-coding gene which contains a selenocysteine (Sec) residue at its active site. Theselenocysteine is encoded by the UGA codon that usually signals translation termination. The 3' UTR ofselenoprotein genes have a conventional stem-loop structure, the sec insertion sequence (SECIS), which isnecessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies in mouse propose thatthis selenoprotein may have redox function and may be implicated in the quality control of protein folding. This geneis localized on chromosome 1p31, a genetic locus usually mutated or deleted in human cancers.Diseases associated with SEP15 include lung cancer susceptibility, and chronic lymphocytic leukemia.
-
Synonyms
15 KDa Selenoprotein, SEP15.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVSAFGAE FSSEACRELG FSSNLLCSSC DLLGQFNLLQ LDPDCRGCCQ EEAQFETKKL YAGAILEVCG CKLGRFPQVQ AFVRSDKPKL FRGLQIKYVR GSDPVLKLLD DNGNIAEELS ILKWNTDSVE EFLSEKLERI
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 :
NOV HumanDescription:
Nephroblastoma Overexpressed Human Recombinant
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Product # :
CYT-805Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.
Purity
Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.More Info
-
Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
-
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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.
-
Solubility
It is recommended to reconstitute the lyophilized NOV in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK 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.
- View Data Sheet
Name :
CXCL13 Human, HisDescription:
BCA-1/ BLC Human Recombinant, His Tag
C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.
Product # :
CHM-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
BCA 1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 110 amino acids (23-109 a.a) and having a molecular mass of 12.7kDa. BCA 1 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
BCA 1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.
-
Synonyms
C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.
-
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 MGSVLEVYYT SLRCRCVQES SVFIPRRFID RIQILPRGNG CPRKEIIVWK KNKSIVCVDP QAEWIQRMME VLRKRSSSTL PVPVFKRKIP.
-
Background
What is the molecular weight/Mw of CXCL13 HUMAN, HIS Protein?
CXCL13 HUMAN, HIS Protein has a total Mw of 12.7kDa.
What is the source or expression system of CXCL13 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL13 HUMAN, HIS Protein?
CXCL13 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL13 HUMAN, HIS Protein?
The biological functionality of CXCL13 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL13 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSVLEVYYT SLRCRCVQES SVFIPRRFID RIQILPRGNG CPRKEIIVWK KNKSIVCVDP QAEWIQRMME VLRKRSSSTL PVPVFKRKIP.
What applications can CXCL13 HUMAN, HIS Protein be used in?
CXCL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL13 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL13 HUMAN, HIS 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 :
CCL24 HumanDescription:
Eotaxin-2 Human Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-238Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CCL24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8.8 kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.More Info
-
Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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.
-
Solubility
It is recommended to reconstitute the lyophilized CCL24 Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
DPKQEWV QRYMKNLDAKQKKASPRARAVA. -
Background
What is the molecular weight/Mw of CCL24 HUMAN Protein?
CCL24 HUMAN Protein has a total Mw of 8.8kDa.
What is the source or expression system of CCL24 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL24 HUMAN Protein?
CCL24 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.
What is the amino acid sequence of CCL24 HUMAN Protein?
VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
DPKQEWV QRYMKNLDAKQKKASPRARAVA.
What applications can CCL24 HUMAN Protein be used in?
CCL24 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 HUMAN Protein?
The endotoxin level is minimal, CCL24 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 :
Platelet Factor 4 MouseDescription:
Platelet Factor-4 Mouse Recombinant (CXCL4)
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-245Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CXCL4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.2kDa.
Source
Escherichia Coli.
Formulation
The Mouse CXCL4 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 1.5M 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 neutrophils using a concentration range of 10-100ng/ml.
More Info
-
Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily.
-
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized CXCL4 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CXCL4 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.
-
Solubility
It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.
-
Background
What is the molecular weight/Mw of PLATELET FACTOR 4 MOUSE Protein?
PLATELET FACTOR 4 MOUSE Protein has a total Mw of 8.2kDa.
What is the source or expression system of PLATELET FACTOR 4 MOUSE Protein?
Escherichia Coli.
What is the Purity of PLATELET FACTOR 4 MOUSE Protein?
PLATELET FACTOR 4 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of PLATELET FACTOR 4 MOUSE Protein?
Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.
What is the amino acid sequence of PLATELET FACTOR 4 MOUSE Protein?
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.
What applications can PLATELET FACTOR 4 MOUSE Protein be used in?
PLATELET FACTOR 4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for PLATELET FACTOR 4 MOUSE Protein?
The endotoxin level is minimal, PLATELET FACTOR 4 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.