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1000 results found for “Cofilin”
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Name :
Leptin BovineDescription:
Leptin Bovine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-502Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin 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 sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation 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. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Resistin Human, AntagonistDescription:
Resistin Antagonist Human Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1255Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Resistin Human antagonist is a monomeric C7A mutant that does not form covalent dimers. Resistin Human antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Resistin was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
(c) Analysis by RP-HPLC.
Biological Activity
The biological activity was evidenced by resistin antagonist activity to inhibit resistin-induced Akt phosphorylation in two cell lines. It also reduced the weight (mainly the visceral fat) and normalized GTT and ITT inHFD-fed mice.
More Info
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Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse 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 Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first seven N-terminal amino acids was determined and was found to be Ala-Ser-Ser-Lys-Thr-Leu-Ala.
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Background
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis. Resistin blocks insulin stimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of low-density lipoprotein (LDL), increasing the risk of heart disease.
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 :
GAL HumanDescription:
Galanin Prepropeptide Human Recombinant
GALN, GLNN, GMAP, GAL, GAL1.
Product # :
PRO-1433Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.
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Synonyms
GALN, GLNN, GMAP, GAL, GAL1.
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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 MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.
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 :
CoV HKU1 HumanDescription:
Coronavirus HKU1 Nucleoprotein Human Recombinant
Product # :
SARS-055Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Coronavirus HKU1 Nucleoprotein is full length protein except the predicted signal peptide of the first 30 aa produced in E.coli and migrate at 50kDa.The CoV HKU1 is fused to a 6xHis tag at its C terminal and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
CoV HKU1 protein solution contains PBS and 25mM K2CO3.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
CoV HKU1 is 1 from 7 known coronaviruses to infect humans including CoV-229E, CoV-NL63, CoVHKU1, MERS-CoV, the original SARS-CoV1, and SARS-CoV-2 (Covid 19). CoV-229E, beta-coronavirus, NL63, CoV-HKU1 and OC43 are the viruses responsible for the common cold. Beta-coronaviruses has an additional shorter spike-like protein called hemagglutinin esterase. Human coronavirus HKU1 (CoV-HKU1) belongs to beta-coronavirus which are enveloped, positive-sense, single stranded RNA and enters its host celll by binding to the N-acetyl9-O-acetyl neuraminic acid 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
SERNYQTFNR GRKTQPKFTV STQPQGNTIP HYSWFSGITQ FQKGRDFKFS DGQGVPIAFG VPPSEAKGYW YRHSRRSFKT ADGQQKQLLP RWYFYYLGTG PYANASYGES LEGVFWVANH QADTSTPSDV SSRDPTTQEA IPTRFPPGTI LPQGYYVEGS GRSASNSRPG SRSQSRGPNN RSLSRSNSNF RHSDSIVKPD ADEIANLVL AKLGKESKPQ QVTKQNAKEI RHKILTKPRQ KRTPNKHCNV QQCFGKRGPS QNFGNAEMLK LGTNDPQFPI LAELAPTPGA FFFGSKLDLV KRDSEADSPV KDVFELHYSG SIRFDSTLPG FETIMKVLEE NLNAYVNSNQ NTDSDSLSSK PQRKRGVKQL PEQFDSLNLS AGTQHISNDF TPEDHSLLAT LDDPYVEDSV A
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Applications
Immunoassay.
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 :
CXCL8 Human (1-72)Description:
Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-231Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.
What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
What applications can CXCL8 HUMAN (1-72) Protein be used in?
CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-72) 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 :
ASF1A HumanDescription:
ASF1 Anti-Silencing Function 1 Homolog A Human Recombinant
CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.
Product # :
PRO-682Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-204 a.a.) and having a molecular mass of 27kDa.ASF1A is fused to a 36 amino acid His Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASF1A protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.
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Synonyms
CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAKV QVNNVVVLDN PSPFYNPFQF EITFECIEDL SEDLEWKIIY VGSAESEEYD QVLDSVLVGP VPAGRHMFVF QADAPNPGLI PDADAVGVTV VLITCTYRGQ EFIRVGYYVN NEYTETELRE NPPVKPDFSK LQRNILASNPRVTRFHINWE DNTEKLEDAE SSNPNLQSLL STDALPSASK GWSTSENSLN VMLESHMDCM.
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 :
EFNA1 Human, HEKDescription:
Ephrin A1 Human Recombinant, HEK
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-2477Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).
Source
HEK293 cells.
Formulation
EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
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Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS 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.
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Name :
EFNB1 Human, Sf9Description:
Ephrin-B1 Human Recombinant, Sf9
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
Product # :
PRO-2543Price :
Quantity :
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Shipped with Ice Packs
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Description
EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.
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Synonyms
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCM2 HumanDescription:
Cerebral Cavernous Malformation 2 Human Recombinant
Cerebral Cavernous Malformation 2, C7orf22, malcavernin, Cerebral Cavernous Malformations 2 Protein, Chromosome 7 Open Reading Frame 22, OSM, MGC4067.
Product # :
PRO-1825Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (66-353 a.a) and having a molecular mass of 34.3kDa.CCM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCM2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cerebral Cavernous Malformation 2, also known as CCM2 is a piece of the CCM signaling pathway which is a vital regulator of heart and vessel formation as well as integrity. CCM2 performs through the stabilization of endothelial cell junctions. In addition, CCM2 functions as a scaffold protein for MAP2K3-MAP3K3 signaling. CCM2 plays a key role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock. Mutations in CCM2 result in cerebral cavernous malformations. Multiple transcript variants encoding dissimilar isoforms have been discovered for CCM2.
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Synonyms
Cerebral Cavernous Malformation 2, C7orf22, malcavernin, Cerebral Cavernous Malformations 2 Protein, Chromosome 7 Open Reading Frame 22, OSM, MGC4067.
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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 MGSEVKYLGQ LTSIPGYLNP SSRTEILHFI DNAKRAHQLP GHLTQEHDAV LSLSAYNVKL AWRDGEDIIL RVPIHDIAAV SYVRDDAAHL VVLKTDDSST KVDIKETYEV EASTFCFPES VDVGGASPHS KTISESELSA SATELLQDYM LTLRTKLSSQ EIQQFAALLH EYRNGASIHE FCINLRQLYG DSRKFLLLGL RPFIPEKDSQ HFENFLETIG VKDGRGIITD SFGRHRRALS TTSSSTTNGN RATGSSDDRS APSEGDEWDR MISDISSDIE ALGCSMDQDS A
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 :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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 MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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 :
LTF Human S.PlasmaDescription:
Lactoferrin Human (Seminal Plasma)
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Product # :
PRO-1591Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- formulation
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Description
The Human Lactoferrin produced from pooled Human seminal plasma has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.
Source
Human seminal plasma.
Formulation
LTF protein filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Purity greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.
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Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK DKSPKFQLFG SPSGQKDLLF KDSAIGFSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALVLKGEAD AMSLDGGYVY TAGKCGLVPV LAENYKSQQS SDPDPNCVDR PVEGYLAVAV VRRSDTSLTW NSVKGKKSCH TAVDRTAGWN IPMGLLFNQT GSCKFDEYFS QSCAPGSDPR SNLCALCIGD EQGENKCVPN SNERYYGYTG AFRCLAENAG DVAFVKDVTV LQNTDGNNNE AWAKDLKLAD FALLCLDGKR KPVTEARSCH LAMAPNHAVV SRMDKVERLK QVLLHQQAKF GRNGSDCPDK FCLFQSETKN LLFNDNTECL ARLHGKTTYE KYLGPQYVAG ITNLKKCSTS PLLEACEFLR K.
-
Human Virus Test
Samples from each donor have been tested and found negative for HBsAg, HIV-1+2, HCV, syphilis, aHBc, RRR.
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 :
GRPEL1 HumanDescription:
GrpE-Like 1 Human Recombinant
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
Product # :
PRO-263Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GRPEL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (28-217a.a.) and having a molecular mass of 23.6kDa.GRPEL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRPEL1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
-
Synonyms
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
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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).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCTATKQKNS GQNLEEDMGQ SEQKADPPAT EKTLLEEKVK LEEQLKETVE KYKRALADTE NLRQRSQKLV EEAKLYGIQA FCKDLLEVAD VLEKATQCVP KEEIKDDNPH LKNLYEGLVM TEVQIQKVFT KHGLLKLNPV GAKFDPYEHE ALFHTPVEGK EPGTVALVSK VGYKLHGRTL RPALVGVVKE A
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 :
CNPY1 HumanDescription:
Canopy FGF Signaling Regulator 1 Human Recombinant
Protein canopy homolog 1, CNPY1.
Product # :
PRO-1872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
CNPY1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-92 a.a) and having a molecular mass of 13.3kDa. CNPY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNPY1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Canopy FGF Signaling Regulator 1, also known as CNPY1, is expressed in the midbrain-hindbrain (MHB) boundary in zebrafish. CNPY1, which binds FGFR1, also takes part in FGF signaling.
-
Synonyms
Protein canopy homolog 1, CNPY1.
-
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 MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL.
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 :
PhI p 2Description:
Pollen allergen Phl p 2 Recombinant
Pollen allergen Phl p 2, Allergen Phl p II, Phl p 2, PHLPII.
Product # :
PRO-2306Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Pollen allergen Phl p 2 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 14,734 Dalton. PhI p 2 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PhI p 2 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Pollen allergen Phl p 2 (PhI p 2) causes an allergic reaction in humans.
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Synonyms
Pollen allergen Phl p 2, Allergen Phl p II, Phl p 2, PHLPII.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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Molar extinction coefficient
15470; A280(1mg/ml)=1.269
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 :
MIF HumanDescription:
Macrophage Migration Inhibitory Factor Human Recombinant
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-575Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Macrophage Inducing Factor Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids (1-115aa) and having a molecular mass of 12kDa. MIF human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 50mM Tris-HCl pH-8, 0.5mM DTT & 10% glycerol.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
-
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
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.
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 :
SDHAF2 HumanDescription:
Succinate Dehydrogenase Complex Assembly Factor 2 Human Recombinant
Succinate dehydrogenase assembly factor 2 mitochondrial, SDH assembly factor 2, Succinate dehydrogenase subunit 5, mitochondrial, hSDH5, SDHAF2, C11orf79, PGL2, SDH5.
Product # :
PRO-593Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
SDHAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (30-166 a.a) and having a molecular mass of 19kDa.SDHAF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDHAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 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
Succinate Dehydrogenase Complex Assembly Factor 2 (SDHAF2) is a mitochondrial protein required for the flavination of a succinate dehydrogenase complex subunit essential for activity of the complex. DHAF2 is necessary for insertion of FAD cofactor into SDHA, the catalytic subunit of succinate dehydrogenase (SDH). SDH is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDHAF2 gene defects are the cause of hereditary paragangliomas type 2 (PGL2), otherwise known as familial non-chromaffin paragangliomas type 2.
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Synonyms
Succinate dehydrogenase assembly factor 2 mitochondrial, SDH assembly factor 2, Succinate dehydrogenase subunit 5, mitochondrial, hSDH5, SDHAF2, C11orf79, PGL2, SDH5.
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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
MGSSHHHHHH SSGLVPRGSH MGSSFRRFYR GDSPTDSQKD MIEIPLPPWQ ERTDESIETK RARLLYESRK RGMLENCILL SLFAKEHLQH MTEKQLNLYD RLINEPSNDW DIYYWATEAK PAPEIFENEV MALLRDFAKN KNKEQRLRAP DLEYLFEKPR.
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 :
SH3GLB2 HumanDescription:
SH3-domain GRB2-like endophilin B2 Human Recombinant
PP6569, PP9455, Endophilin-B2, KIAA1848, SH3 domain-containing GRB2-like protein B2.
Product # :
PRO-1287Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SH3GLB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-395a.a.) and having a molecular mass of 46.4 kDa. SH3GLB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SH3GLB2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Endophilin-B2 (SH3GLB2) belongs to the endophilin B subgroup. The endophilins comprise a family of proteins that relates with amphiphysin, synaptojanin and dynamin and are involved in presynaptic vesicle trafficking at nerve terminals.The expression patterns of the endophilins are coherent with their cellular functions at the neuronal synapse. SH3GLB2 is ubiquitously expressed however presents highest levels in brain, adult lung, ovary, and spinal cord.Low levels of SH3GLB2 are found in Down syndrome and reflect brain dysgenesis.
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Synonyms
PP6569, PP9455, Endophilin-B2, KIAA1848, SH3 domain-containing GRB2-like protein B2.
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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
MGSSHHHHHH SSGLVPRGSH MGSMDFNMKK LASDAGIFFT RAVQFTEEKF GQAEKTELDA HFENLLARAD STKNWTEKIL RQTEVLLQPN PSARVEEFLY EKLDRKVPSR VTNGELLAQY MADAASELGP TTPYGKTLIK VAEAEKQLGA AERDFIHTAS ISFLTPLRNF LEGDWKTISK ERRLLQNRRL DLDACKARLK KAKAAEAKAT TVPDFQETRP RNYILSASAS ALWNDEVDKA EQELRVAQTE FDRQAEVTRL LLEGISSTHV NHLRCLHEFV KSQTTYYAQC YRHMLDLQKQ LGRFPGTFVG TTEPASPPLS STSPTTAAAT MPVVPSVASL APPGEASLCL EEVAPPASGT RKARVLYDYE AADSSELALL ADELITVYSL PGMDPDWLIG ERGNKKGKVP VTYLELLS.
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 :
EG VEGF HumanDescription:
Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant
PK1, PRK1, Prokineticin 1, EG-VEGF.
Product # :
CYT-338Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
More Info
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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
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Synonyms
PK1, PRK1, Prokineticin 1, EG-VEGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor 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
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
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Background
Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications
Abstract:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.Introduction:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.Production and Characterization:
Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.Role in Endocrine Disorders:
EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.Therapeutic Implications:
Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.Conclusion:
Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.7kDa.
What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.
What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EG-VEGF Protein?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF 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 :
SRGN HumanDescription:
Serglycin Human Recombinant
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Product # :
PRO-965Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
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Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.
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 :
OCIAD2 HumanDescription:
OCIA Domain Containing 2 Human Recombinant
OCIA domain-containing protein 2, Ovarian carcinoma immunoreactive antigen-like protein, OCIAD2.
Product # :
PRO-1456Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OCIAD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-154 a.a) and having a molecular mass of 19.3kDa.OCIAD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OCIAD2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
OCIA domain-containing protein 2 (OCIAD2) is a protein-coding gene which localizes to endosomes and contains one Ovarian carcinoma immunoreactive antigen (OCIA) domain. Among the associated diseases with OCIAD2 are bronchiolo-alveolar adenocarcinoma, and ovarian mucinous neoplasm. OCIAD1 is an important paralog of this gene.
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Synonyms
OCIA domain-containing protein 2, Ovarian carcinoma immunoreactive antigen-like protein, OCIAD2.
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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
MGSSHHHHHH SSGLVPRGSH MGSMASASAR GNQDKDAHFP PPSKQSLLFC PKSKLHIHRA EISKIMRECQ EESFWKRALP FSLVSMLVTQ GLVYQGYLAA NSRFGSLPKV ALAGLLGFGL GKVSYIGVCQ SKFHFFEDQL RGAGFGPQHN RHCLLTCEEC KIKHGLSEKG DSQPSAS
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 :
Omentin 298 a.a. HumanDescription:
Omentin 298 a.a. Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-061Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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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
MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR
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 :
Streptavidin (37-159), HisDescription:
Streptavidin (37-159 a.a) Recombinant, His Tag
Product # :
PRO-1495Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The Streptavidin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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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 MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.
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 :
CCL6 MouseDescription:
C-10 Mouse Recombinant (CCL6)
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
Product # :
CHM-307Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- biological activity
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Description
C-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.7kDa.The CCL6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCL6 Mouse was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.
More Info
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Introduction
Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1. -
Synonyms
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized C10 protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL6 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 C10 protein 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
GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.
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Background
What is the molecular weight/Mw of CCL6 MOUSE Protein?
CCL6 MOUSE Protein has a total Mw of 10.7kDa.
What is the source or expression system of CCL6 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL6 MOUSE Protein?
CCL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL6 MOUSE Protein?
The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.
What is the amino acid sequence of CCL6 MOUSE Protein?
GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.
What applications can CCL6 MOUSE Protein be used in?
CCL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL6 MOUSE Protein?
The endotoxin level is minimal, CCL6 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CALB1 RatDescription:
Calbindin-1 Rat Recombinant
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, Spot 35 protein, Calb1, CaBP28K, MGC93326.
Product # :
PRO-400Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Recombinant Rat Calbindin-1 produced in E.Coli.The Rat CALB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution (1mg/ml) containing 50mM NaHCO3.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Calbindins are Ca-binding proteins belonging to the troponin C superfamily. CALB28K/Calbindin1/CALB1 (D28K/Spot35 protein or cholecalcin, rat 261 aa; mouse 261 aa; human 261-aa, chromosome 8q21.3-q22.1) was originally described as 27-kDA induced by vitamin D in the duodenum of chicken. In mammals, it is expressed in the kidney, pancreatic islets, and brain. In brain, its synthesis is independent of vitamin D. CABP28K contains 4 active and 2 inactive EF-hand Ca-binding domains. The gene for CABP28K is clustered in the same region as carbonic anhydrase. The neurons in the brains of patients with Huntington disease are CAB28K depleted. There are two types of CaBPs: the "trigger"- and the "buffer"-CaBPs. The conformation of "trigger" type CaBPs changes upon Ca2+ binding and exposes regions on protein that interact with target molecules, thus altering their activity. The buffer-type CABP are thought to control the intracellular calcium concentration. Calbindin D-28K is found predominantly in subpopulations of central and peripheral nervous system neurons, and in certain epithelial cells involved in Ca2+ transport such as distal tubular cells and cortical collecting tubules of the kidney, and in enteric neuroendocrine cells.
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Synonyms
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, Spot 35 protein, Calb1, CaBP28K, MGC93326.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CABP28K although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CABP28K 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 CABP28K in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
CABP28K can be used for immunoblots, absorption experiments in immunohistochemistry, radioimmunoassay and intracellular injection.
For adsorption we suggest the following procedureA- Dilute 1 µl of the monoclonal antibody against calbindin D-28k in 5 ml of the usual buffer for immunohistochemistry (final dilution 1:5'000).
B- Add 1 µg of the recombinant protein to 1 ml of the diluted antibody solution and mix well.
C- Incubate for at least 6 hours in the cold.
D- Apply to tissue-sections and incubate for 3 days.
E- Complete the immunohistochemical reaction as usual (biotinylated second antibody, ABC-complex, DAB).
As a result, the immunostaining should be strongly reduced or even completely prevented.
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.