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Name :
CXCL14 HumanDescription:
BRAK (CXCL14) Human Recombinant
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Product # :
CHM-001Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized after extensive dialysis against 20mM Tris-HCl, pH 8.5 and 1M NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.
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Background
What is the molecular weight/Mw of CXCL14 HUMAN Protein?
CXCL14 HUMAN Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL14 HUMAN Protein?
CXCL14 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 HUMAN Protein?
The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.
What applications can CXCL14 HUMAN Protein be used in?
CXCL14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 HUMAN Protein?
The endotoxin level is minimal, CXCL14 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KISS1 HumanDescription:
KISS-1 Metastasis-Suppressor Human Recombinant
Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.
Product # :
PRO-419Price :
Quantity :
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Shipped with Ice Packs
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Description
KISS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (20-138) and having a molecular mass of 12.6 Dalton. The KISS1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein 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
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Introduction
KISS1 is a metastasis suppressor protein that suppresses metastases of melanomas and breast carcinomas without affecting tumorigenicity.KISS1 functions to inhibit chemotaxis and invasion, attenuating metastasis in malignant melanomas. KISS1 is involved in the regulation of cell-matrix adhesion. KISS1 plays a role in cytoskeletal reorganization. A polymorphism in the terminal exon of KISS1 mRNA results in two protein isoforms. Expression of KiSS1 is localized to specific regions of the hypothalamus in numerous species and is regulated by gonadal steroids and across the estrous cycle..KISS1 generates a c-terminally amidated peptide, metastin which functions as the endogenous ligand of the g-protein coupled receptor gpr54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis.
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Synonyms
Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MEPLEKVASV GNSRPTGQQL ESLGLLAPGE QSLPCTERKP AATARLSRRG TSLSPPPESS GSPQQPGLSA PHSRQIPAPQ GAVLVQREKD LPNYNWNSFG LRFGKREAAP GNHGRSAGRG.
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 :
TXN1 Human, HisDescription:
Thioredoxin Human Recombinant, His Tag
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-804Price :
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Shipped with Ice Packs
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Description
Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TXN1 solution containing 1x PBS pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.More Info
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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
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Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
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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 MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.
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 :
PSMA7 HumanDescription:
Proteasome Subunit Alpha Type 7 Human Recombinant
HSPC, RC6-1, XAPC7, MGC3755, PSMA-7, Proteasome subunit alpha type-7, Proteasome subunit RC6-1, Proteasome subunit XAPC7, PSMA7, C6.
Product # :
ENZ-403Price :
Quantity :
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Shipped with Ice Packs
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Description
PSMA7 Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-248) and having a molecular mass of 30kDa. PSMA7 is fused to a 20 amino acid His Tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The PSMA7 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, and 20% glycerol.
Purity
Greater than 90.0% as determined SDS-PAGE.
More Info
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Introduction
The proteasome is a multicatalytic proteinase complex with a highly assembled ring-shaped 20S core structure which is composed of 4 rings of 28 non-identical subunits, 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are found throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. PSMA7 is part of the peptidase T1A family, that is a 20S core alpha subunit. PSMA7 interacts particularly with the hepatitis B virus X protein, a protein critical to viral replication. PSMA7 is involved in regulating hepatitis virus C internal ribosome entry site activity that is crucial for viral replication. PSMA7 is in charge for regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. PSMA7 is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. PSMA7 interacts specifically with two subdomains of HIF-1alpha and inhibited the transactivation function of HIF-1alpha under both normoxic and hypoxia-mimicking conditions.
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Synonyms
HSPC, RC6-1, XAPC7, MGC3755, PSMA-7, Proteasome subunit alpha type-7, Proteasome subunit RC6-1, Proteasome subunit XAPC7, PSMA7, C6.
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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 MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS.
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 :
PSMD5 HumanDescription:
Proteasome 26S Subunit, Non-ATPase 5 Human Recombinant
PSMD5, Proteasome (Prosome, Macropain) 26S Subunit, Non-ATPase, 526S Protease Subunit S5 Basic,26S Proteasome Subunit S5B,S5B,26S Proteasome Non-ATPase Regulatory Subunit 5,KIAA0072.
Product # :
ENZ-914Price :
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Shipped with Ice Packs
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Description
PSMD5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 529 amino acids (1-504 a.a) and having a molecular mass of 58.9kDa.PSMD5 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PSMD5 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Proteasome 26S Subunit, Non-ATPase 5, also known as PSMD5 is a member of the proteasome subunit S5B/HSM3 family. The 26S proteasome is an enzymatic complex which degrades ubiquitinated proteins in eukaryotic cells. Furthermore, PSMD5 acts as a chaperones which is involved in the assembly of the 26s proteasome, particularly of the base subcomplex of the PA700/19S regulatory complex. PSMD5 is full of dileucine repeats, which have been involved in trafficking of various transmembrane proteins.
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Synonyms
PSMD5, Proteasome (Prosome, Macropain) 26S Subunit, Non-ATPase, 526S Protease Subunit S5 Basic,26S Proteasome Subunit S5B,S5B,26S Proteasome Non-ATPase Regulatory Subunit 5,KIAA0072.
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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 MGSEFMAAQA LALLREVARL EAPLEELRAL HSVLQAVPLN ELRQQAAELR LGPLFSLLNE NHREKTTLCV SILERLLQAM EPVHVARNLR VDLQRGLIHP DDSVKILTLS QIGRIVENSD AVTEILNNAE LLKQIVYCIG GENLSVAKAA IKSLSRISLT QAGLEALFES NLLDDLKSVM KTNDIVRYRV YELIIEISSV SPESLNYCTT SGLVTQLLRE LTGEDVLVRA TCIEMVTSLA YTHHGRQYLA QEGVIDQISN IIVGADSDPF SSFYLPGFVK FFGNLAVMDS PQQICERYPI FVEKVFEMIE SQDPTMIGVA VDTVGILGSN VEGKQVLQKT GTRFERLLMR IGHQSKNAPV ELKIRCLDAI SSLLYLPPEQ QTDDLLRMTE SWFSSLSRDP LELFRGISSQ PFPELHCAAL KVFTAIANQP WAQKLMFNSP GFVEYVVDRS VEHDKASKDA KYELVKALAN SKTIAEIFGN PNYLRLRTYL SEGPYYVKPV STTAVEGAE.
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 :
Leptin Human, MutantDescription:
Leptin Mutant D23L Human Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Leptin Mutant was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Mutant D23L is fully biologically 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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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Mutant D23L although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant 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.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Mutant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids of recombinant human leptin was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GCSF MonkeyDescription:
Granulocyte Colony Stimulating Factor Recombinant Rhesus Macaque
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Product # :
CYT-1121Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.GCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.
More Info
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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
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Synonyms
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque 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 Granulocyte Colony Stimulating Rhesus Macaque 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
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
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Background
What is the molecular weight/Mw of GCSF MONKEY Protein?
GCSF MONKEY Protein has a total Mw of 18.9kDa.
What is the source or expression system of GCSF MONKEY Protein?
Escherichia Coli.
What is the Purity of GCSF MONKEY Protein?
GCSF MONKEY Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GCSF MONKEY Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.
What is the amino acid sequence of GCSF MONKEY Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
What applications can GCSF MONKEY Protein be used in?
GCSF MONKEY Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GCSF MONKEY Protein?
The endotoxin level is minimal, GCSF MONKEY 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 :
SELE Human, HEKDescription:
E-Selectin Human Recombinant, HEK
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
Product # :
PRO-1645Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SELE although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELE 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 SELE in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.
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 :
HMBS HumanDescription:
Hydroxymethylbilane Synthase Human Recombinant
Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.
Product # :
ENZ-581Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HMBS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-361) and having a molecular mass of 41.9kDa.HMBS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HMBS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.
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Synonyms
Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.
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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 MGSHMSGNGN AAATAEENSP KMRVIRVGTR KSQLARIQTD SVVATLKASY PGLQFEIIAM STTGDKILDT ALSKIGEKSL FTKELEHALE KNEVDLVVHS LKDLPTVLPP GFTIGAICKR ENPHDAVVFH PKFVGKTLET LPEKSVVGTS SLRRAAQLQR
KFPHLEFRSI RGNLNTRLRK LDEQQEFSAI ILATAGLQRM GWHNRVGQIL HPEECMYAVG QGALGVEVRA KDQDILDLVG VLHDPETLLR CIAERAFLRH LEGGCSVPVA VHTAMKDGQL YLTGGVWSLD GSDSIQETMQ ATIHVPAQHE DGPEDDPQLV GITARNIPRG PQLAAQNLGI
SLANLLLSKG AKNILDVARQ LNDAH.
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 :
CXCL14 RatDescription:
BRAK (CXCL14) Rat Recombinant
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Product # :
CHM-021Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 RAT Protein?
CXCL14 RAT Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL14 RAT Protein?
CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 RAT Protein?
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 RAT Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 RAT Protein be used in?
CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 RAT Protein?
The endotoxin level is minimal, CXCL14 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 :
FAM50A HumanDescription:
Family with Sequence Similarity 50, Member A Human Recombinant
9F, DXS9928E, HXC-26, HXC26, XAP5, XAP-5.
Product # :
PRO-1477Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FAM50A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (150-339 a.a.) and having a molecular mass of 25.2kDa.FAM50A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
FAM50A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
FAM50A is a member of the FAM50 family. FAM50A is highly conserved in length and sequence among numerous species. FAM50A is a basic protein comprised of a nuclear localization signal, and can function as a DNA-binding protein or a transcriptional factor. FAM50A expressed in all tissues mainly abundant in fetal brain, liver and kidney. High levels of FAM50A were observed in the adult's skeletal muscle, spleen, thymus, prostate and the small intestine.
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Synonyms
9F, DXS9928E, HXC-26, HXC26, XAP5, XAP-5.
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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 MGSTTKKRKL GKNPDVDTSF LPDRDREEEE NRLREELRQE WEAKQEKIKS EEIEITFSYW DGSGHRRTVK MRKGNTMQQF LQKALEILRK DFSELRSAGV EQLMYIKEDL IIPHHHSFYD FIVTKARGKS GPLFNFDVHD DVRLLSDATV EKDESHAGKV VLRSWYEKNK HIFPASRWEP YDPEKKWDKY TIR.
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 :
TFF2 Human, HisDescription:
Trefoil Factor-2 Human Recombinant, His Tag
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
Product # :
CYT-611Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids (24-129) which includes a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 13.2 kDa. TFF2 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5, and 20mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.
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Synonyms
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.
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 :
CX3CL1 RatDescription:
Fractalkine Rat Recombinant (CX3CL1)
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-005Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fractalkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa.The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FractalkineRat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fractalkine 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 Fractalkine 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
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
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Background
What is the molecular weight/Mw of CX3CL1 RAT Protein?
CX3CL1 RAT Protein has a total Mw of 8.7kDa.
What is the source or expression system of CX3CL1 RAT Protein?
Escherichia Coli.
What is the Purity of CX3CL1 RAT Protein?
CX3CL1 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 RAT Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.
What is the amino acid sequence of CX3CL1 RAT Protein?
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
What applications can CX3CL1 RAT Protein be used in?
CX3CL1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 RAT Protein?
The endotoxin level is minimal, CX3CL1 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.
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Name :
LGALS7 Human, HisDescription:
Galectin-7 Human Recombinant, His Tag
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
Product # :
CYT-617Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
Galectin-7 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 156 amino acids (1-136 a.a.) and having a molecular mass of 17.2kDa. The Galectin-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-7 solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.
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Synonyms
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
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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 MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.
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Background
What is the molecular weight/Mw of LGALS7 HUMAN, HIS Protein?
LGALS7 HUMAN, HIS Protein has a total Mw of 17.2kDa.
What is the source or expression system of LGALS7 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS7 HUMAN, HIS Protein?
LGALS7 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS7 HUMAN, HIS Protein?
The biological functionality of LGALS7 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of LGALS7 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.
What applications can LGALS7 HUMAN, HIS Protein be used in?
LGALS7 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS7 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS7 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 :
PF4 BovineDescription:
Platelet Factor-4 (CXCL4) Bovine Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-039Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- purity
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Description
Platelet Factor-4 (CXCL4) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 88 amino acid and having a molecular mass of approximately 9.5kDa.PF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets.PF4’s major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III 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 chemokine family. Furthermore, it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Platelet Factor-4 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 Platelet Factor-4 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
ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.
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 :
HSPBP1 HumanDescription:
Heat Shock Protein-Binding Protein 1 Human Recombinant
Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.
Product # :
HSP-030Price :
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Shipped with Ice Packs
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Description
HSPBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 382 amino acids (1-362 a.a.) and having a molecular mass of 41.6kDa. HSPBP1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HSPBP1 solution containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol, 2mM EDTA and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Hsp70-binding protein 1 (HSPBP1) is a member of a family of eukaryotic proteins identified as nucleotide exchange factors for HSP 70 that exhibit varying degrees of compartment and species specificity. HSPBP1 is localized mainly in cytoplasm and nucleus but is also found extracellularly. HSPBP1 is mostly expressed in heart and skeletal muscle .HSPBP1 binds to HSP 70, inhibits its activity and promotes dissociation of nucleotides from the HSP 70 ATPase domain. In addition, HSPBP1 inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and obstructing the ATP binding. HSPBP1 may also have a role in tumor (dys)regulation of chaperone proteins. Furthermore, HSPBP1 hinders ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.
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Synonyms
Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
HSPBP1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM DR.
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 :
EFNB3 Human, Sf9Description:
Ephrin- B3 Human Recombinant, Sf9
Ephrin B3, EPH-Related Receptor Transmembrane Ligand ELK-L3, Ephrin-B3, EPLG8, LERK8, Eph-Related Receptor Tyrosine Kinase Ligand 8, EPH-Related Receptor Tyrosine Kinase Ligand 8, LERK-8, EFL6, Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8.
Product # :
PRO-2381Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EFNB3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 208 amino acids (28-226a.a.) and having a molecular mass of 23.0kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). EFNB3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.
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Synonyms
Ephrin B3, EPH-Related Receptor Transmembrane Ligand ELK-L3, Ephrin-B3, EPLG8, LERK8, Eph-Related Receptor Tyrosine Kinase Ligand 8, EPH-Related Receptor Tyrosine Kinase Ligand 8, LERK-8, EFL6, Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8.
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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
ADPLSLEPVY WNSANKRFQA EGGYVLYPQI GDRLDLLCPR ARPPGPHSSP NYEFYKLYLV GGAQGRRCEA PPAPNLLLTC DRPDLDLRFT IKFQEYSPNL WGHEFRSHHD YYIIATSDGT REGLESLQGG VCLTRGMKVL LRVGQSPRGG AVPRKPVSEM PMERDRGAAH SLEPGKENLP GDPTSNATSR GAEGPLPPPS MPHHHHHH.
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 :
PLDN HumanDescription:
Pallidin Homolog Human Recombinant
Pallidin protein homolog (mouse), PA, HPS9, PALLID, syntaxin 13-interacting protein pallid.
Product # :
PRO-1068Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PLDN Human Recombinant produced in E. coli is a single polypeptide chain containing 192 amino acids (1-172) and having a molecular mass of 21.9kDa.PLDN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PLDN solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Pallidin is involved in intracellular vesicle trafficking. PLDN cooperates with Syntaxin 13 that facilitates intracellular membrane fusion. A Few alternatively spliced transcript variations of this gene have been discovered however the full-length nature of several of these variants has not been determined. PLDN takes part in the creation of lysosome-related organelles, for example melanosomes and platelet-dense granules. PLDN is known to cooperate with Dysbindin, BLOC1S1, STX12, CNO, MUTED, SNAPAP and BLOC1S2.
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Synonyms
Pallidin protein homolog (mouse), PA, HPS9, PALLID, syntaxin 13-interacting protein pallid.
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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 MSVPGPSSPD GALTRPPYCL EAGEPTPGLS DTSPDEGLIE DLTIEDKAVE QLAEGLLSHY LPDLQRSKQA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFAEAKH YHAKLVNIRK EMLMLHEKTS KLKKRALKLQ QKRQKEELER EQQREKEFER EKQLTARPAK RM
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 :
Procalcitonin HumanDescription:
Procalcitonin Human Recombinant
Procalcitonin, PCT.
Product # :
HOR-304Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Procalcitonin, PCT.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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 procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.
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 :
VEGF Human (121 a.a.), HisDescription:
Vascular Endothelial Growth Factor-121 Human Recombinant, His Tag
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-619Price :
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Shipped with Ice Packs
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Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain (aa 207-327) containing a total of 142 amino acids and having a molecular mass of 16.3 kDa. The VEGF-121 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VEGF-121 His Tag in 20mM Tris pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is <4.2 ng/ml. Measured in a cell proliferation assay using NIH-3T3 cell, corresponding to a specific activity of less than 238,095.23units/mg.More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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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 MAPMAEGGGQ NHHEVVKFMD VYQRSYCHPI ETLVDIFQEY PDEIEYIFKP SCVPLMRCGG CCNDEGLECV PTEESNITMQ IMRIKPHQGQ HIGEMSFLQH NKCECRPKKD RARQEKCDKP RR.
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 :
TROVE2 Human, His BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, His Tag Biotinylated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2560Price :
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Shipped with Ice Packs
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Description
TROVE2 Human Recombinant Biotin produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 56kDa. The TROVE2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM HEPES (pH 8.0), 20% Glycerol and 150mM NaCl.
Purity
Greater than 89% as determined by Capillary Electrophoresis.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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 :
Y.Enterocolitica (O:8) YopMDescription:
Yersinia Enterocolitica (O:8) YopM Recombinant
Product # :
PRO-2272Price :
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Description
Recombinant Yersinia Enterocolitica (O:8) YopM produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 60,898 Dalton. Y.Enterocolitica (O:8) YopM is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica(O:8) YopM is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.
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 :
SERPINB3 HumanDescription:
Serpin Peptidase Inhibitor, Clade B Member 3 Human Recombinant
Serpin B3, Squamous cell carcinoma antigen 1, Protein T4-A, SCCA-1, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member 3, SCCA1, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member 3, Squamous Cell Carcinoma Antigen 1, Protein T4-A, SCCA-1, Serpin B3, HsT1196, SCCA-PD, T4-A , SCCA, SCC.
Product # :
PRO-2198Price :
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Shipped with Ice Packs
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Description
SERPINB3 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 47kDa. SERPINB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERPINB3 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
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Introduction
Serpin Peptidase Inhibitor, Clade B Member 3, also known as SERPINB3 is a papain-like cysteine protease inhibitor which modulates the host immune response versus tumor cells. SERPINB3 is a protein coding gene which acts as an inhibitor of UV-induced apoptosis by suppressing the activity of c-Jun NH(2)-terminal kinase (JNK1).
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Synonyms
Serpin B3, Squamous cell carcinoma antigen 1, Protein T4-A, SCCA-1, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member 3, SCCA1, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member 3, Squamous Cell Carcinoma Antigen 1, Protein T4-A, SCCA-1, Serpin B3, HsT1196, SCCA-PD, T4-A , SCCA, SCC.
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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 MGSMNSLSEA NTKFMFDLFQ QFRKSKENNI FYSPISITSA LGMVLLGAKD NTAQQIKKVL HFDQVTENTT GKAATYHVDR SGNVHHQFQK LLTEFNKSTD AYELKIANKL FGEKTYLFLQ EYLDAIKKFY QTSVESVDFA NAPEESRKKI NSWVESQTNE KIKNLIPEGN IGSNTTLVLV NAIYFKGQWE KKFNKEDTKE EKFWPNKNTY KSIQMMRQYT SFHFASLEDV QAKVLEIPYK GKDLSMIVLL PNEIDGLQKL EEKLTAEKLM EWTSLQNMRE TRVDLHLPRF KVEESYDLKD TLRTMGMVDI FNGDADLSGM TGSRGLVLSG VLHKAFVEVT EEGAEAAAAT AVVGFGSSPT STNEEFHCNH PFLFFIRQNK TNSILFYGRF SSP.
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 :
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
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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.