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1000 results found for “anti coagulation factors”
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Name :
AFP ProteinDescription:
Alpha Fetoprotein Human Recombinant
Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.
Product # :
PRO-2229Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 600 amino acids (19-609a.a.) and having a molecular mass of 67.5kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). AFP is expressed with a ADP at N-terminus and 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AFP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
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Synonyms
Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.
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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
ADPRTLHRNEYGI ASILDSYQCT AEISLADLAT IFFAQFVQEA TYKEVSKMVK DALTAIEKPT GDEQSSGCLE NQLPAFLEEL CHEKEILEKY GHSDCCSQSE EGRHNCFLAH KKPTPASIPL FQVPEPVTSC EAYEEDRETF MNKFIYEIAR RHPFLYAPTI LLWAARYDKI IPSCCKAENA VECFQTKAAT VTKELRESSL LNQHACAVMK NFGTRTFQAI TVTKLSQKFT KVNFTEIQKL VLDVAHVHEH CCRGDVLDCL QDGEKIMSYI CSQQDTLSNK ITECCKLTTL ERGQCIIHAE NDEKPEGLSP NLNRFLGDRD FNQFSSGEKN IFLASFVHEY SRRHPQLAVS VILRVAKGYQ ELLEKCFQTE NPLECQDKGE EELQKYIQES QALAKRSCGL FQKLGEYYLQ NAFLVAYTKK APQLTSSELM AITRKMAATA ATCCQLSEDK LLACGEGAAD IIIGHLCIRH EMTPVNPGVG QCCTSSYANR RPCFSSLVVD ETYVPPAFSD DKFIFHKDLC QAQGVALQTM KQEFLINLVK QKPQITEEQL EAVIADFSGL LEKCCQGQEQ EVCFAEEGQK LISKTRAALG VHHHHHH.
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 :
AZGP1Description:
Alpha-2-Glycoprotein 1 Zinc-Binding Human Recombinant
Zinc-alpha-2-glycoprotein, ZA2G, ZAG, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein.
Product # :
PRO-2169Price :
Quantity :
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Shipped with Ice Packs
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Description
AZGP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (21-298 a.a) and having a molecular mass of 34.5kDa.AZGP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AZGP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc-alpha-2-glycoprotein (AZGP1) protein stimulates lipid degradation in adipocytes and causes the massive fat losses linked with various advanced cancers. AZGP1 may bind polyunsaturated fatty acids.
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Synonyms
Zinc-alpha-2-glycoprotein, ZA2G, ZAG, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQENQDGR YSLTYIYTGL SKHVEDVPAF QALGSLNDLQ FFRYNSKDRK SQPMGLWRQV EGMEDWKQDS QLQKAREDIF METLKDIVEY YNDSNGSHVL QGRFGCEIEN NRSSGAFWKY YYDGKDYIEF NKEIPAWVPF DPAAQITKQK WEAEPVYVQR AKAYLEEECP ATLRKYLKYS KNILDRQDPP SVVVTSHQAP GEKKKLKCLA YDFYPGKIDV HWTRAGEVQE PELRGDVLHN GNGTYQSWVV VAVPPQDTAP YSCHVQHSSL AQPLVVPWEA S.
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 :
NELFE HumanDescription:
Negative Elongation Factor Complex Member E Human Recombinant
Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.
Product # :
PRO-1968Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NELFE Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-380) and having a molecular mass of 45.6 kDa.NELFE is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NELFE solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NELFE is a vital component of NELF complex which represses RNA polymerase II transcript elongation. NELFE is similar to nuclear RNA-binding proteins but does not bind RNA. NELFE contains a tract of alternating basic and acidic residues, mainly arginine and aspartic acid.
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Synonyms
Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.
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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 MGSMLVIPPG LSEEEEALQK KFNKLKKKKK ALLALKKQSS SSTTSQGGVK RSLSEQPVMD TATATEQAKQ LVKSGAISAI KAETKNSGFK RSRTLEGKLK DPEKGPVPTF QPFQRSISAD DDLQESSRRP QRKSLYESFV SSSDRLRELG PDGEEAEGPG AGDGPPRSFD WGYEERSGAH SSASPPRSRS RDRSHERNRD RDRDRERDRD RDRDRDRERD RDRDRDRDRD RERDRDRERD RDRDREGPFR RSDSFPERRA PRKGNTLYVY GEDMTPTLLR GAFSPFGNII DLSMDPPRNC AFVTYEKMES ADQAVAELNG TQVESVQLKV NIARKQPMLD AATGKSVWGS LAVQNSPKGC HRDKRTQIVY SDDVYKENLV DGF.
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 :
MMP 3 HumanDescription:
Matrix Metalloproteinase-3 Human Recombinant
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
Product # :
ENZ-774Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMP 3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (100-477a.a) and having a molecular mass of 45.2kDa. MMP 3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP 3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
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Synonyms
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
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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 MGSFRTFPGI PKWRKTHLTY RIVNYTPDLP KDAVDSAVEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVR EHGDFYPFDG PGNVLAHAYA PGPGINGDAH FDDDEQWTKD TTGTNLFLVA AHEIGHSLGL FHSANTEALM YPLYHSLTDL TRFRLSQDDI NGIQSLYGPP PDSPETPLVP TEPVPPEPGT PANCDPALSF DAVSTLRGEI LIFKDRHFWR KSLRKLEPEL HLISSFWPSL PSGVDAAYEV TSKDLVFIFK GNQFWAIRGN EVRAGYPRGI HTLGFPPTVR KIDAAISDKE KNKTYFFVED KYWRFDEKRN SMEPGFPKQI AEDFPGIDSK IDAVFEEFGF FYFFTGSSQL EFDPNAKKVT HTLKSNSWLN C.
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 :
UrokinaseDescription:
Urokinase Human Recombinant
PLAU, ATF, BDPLT5, QPD, u-PA, UPA, URK, Urokinase-type plasminogen activator, U-plasminogen activator, uPA, Urokinase-type plasminogen activator long chain A, Urokinase-type plasminogen activator short chain A, Urokinase-type plasminogen activator chain B.
Product # :
ENZ-965Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Urokinase Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 419 amino acids (21-431) and having a molecular mass of 47.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).Urokinase is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Urokinase protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture. -
Synonyms
PLAU, ATF, BDPLT5, QPD, u-PA, UPA, URK, Urokinase-type plasminogen activator, U-plasminogen activator, uPA, Urokinase-type plasminogen activator long chain A, Urokinase-type plasminogen activator short chain A, Urokinase-type plasminogen activator chain B.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
SNELHQVPSN CDCLNGGTCV SNKYFSNIHW CNCPKKFGGQ HCEIDKSKTC YEGNGHFYRG KASTDTMGRP CLPWNSATVL QQTYHAHRSD ALQLGLGKHN YCRNPDNRRR PWCYVQVGLK PLVQECMVHD CADGKKPSSP PEELKFQCGQ KTLRPRFKII GGEFTTIENQ PWFAAIYRRH RGGSVTYVCG GSLISPCWVI SATHCFIDYP KKEDYIVYLG RSRLNSNTQG EMKFEVENLI LHKDYSADTL AHHNDIALLK IRSKEGRCAQ PSRTIQTICL PSMYNDPQFG TSCEITGFGK ENSTDYLYPE QLKMTVVKLI SHRECQQPHY YGSEVTTKML CAADPQWKTD SCQGDSGGPL VCSLQGRMTL TGIVSWGRGC ALKDKPGVYT RVSHFLPWIR SHTKEENGLA LLEHHHHHH.
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 :
Prolactin RatDescription:
Prolactin Rat Recombinant
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
Product # :
CYT-322Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6 kDa. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065 ng/ml corresponding to a specific activity of 15,400,000 Units/mg.More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin 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 Met-Leu-Pro-Val-Cys.
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 :
CD57 Biotin AntibodyDescription:
CD57 Biotinylated, Mouse Anti-Human
NK1, CD57, HNK1, LEU7, NK-1, GLCATP, GLCUATP, B3GAT1.
Product # :
ANT-288Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
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Introduction
CD57 also called B3GAT1is part of the glucuronyltransferase gene family. CD57 exhibits strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. CD57 takes part in the glucuronyl transfer reaction during the biosynthesis of the carbohydrate epitope HNK-1.
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Synonyms
NK1, CD57, HNK1, LEU7, NK-1, GLCATP, GLCUATP, B3GAT1.
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Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
Human CD57 Positive Cells.
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Ig Subclass
Mouse IgM.
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Clone
hCD57.
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Applications
Staining antibody. For staining, use 10µl/1,000,000 cells.
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Available Conjugates
This antibody is also available unconjugated and conjugated to FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/1,000,000 cells.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
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Purification Method
Ion-Exchange Column.
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 :
CD31 FITC AntibodyDescription:
CD31-FITC, Mouse Anti Human
Platelet endothelial cell adhesion molecule, PECAM-1, EndoCAM, GPIIA', CD31 antigen, PECAM1, CD31.
Product # :
ANT-052Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
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Introduction
CD31 is a glycoprotein expressed on endothelial cells, platelets, macrophages and Kupffer cells, granulocytes, T / NK cells, lymphocytes, megakaryocytes, fibroblasts, osteoclasts, neutrophils. In humans, the gene encoding CD31 is found on chromosome 17.
CD31 is a cluster of differentiation molecule. It is also called PECAM-1 for platelet endothelial cell adhesion molecule. It plays a key role in removing aged neutrophils from the body. Both the neutrophil and the macrophage express CD31 on their membranes, and during the testing process, these CD31 molecules bind the two cells together. If the neutrophil is healthy, it will send a signal to the macrophage, and the CD31 molecules will detach.
CD31 is also expressed in certain tumors, including epithelioid hemangioendothelioma, epithelioid sarcoma-like hemangioendothelioma, other vascular tumors, histiocytic malignancies, and plasmacytomas. It is rarely found in some sarcomas and carcinomas. -
Synonyms
Platelet endothelial cell adhesion molecule, PECAM-1, EndoCAM, GPIIA', CD31 antigen, PECAM1, CD31.
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Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
Enriched human platelets
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Ig Subclass
mouse IgG1
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Clone
hCD31
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Applications
Flow cytometry, immunohistochemistry. For staining, use 10µl/106 cells.
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Note
CD31 is expressed in high levels on endothelial cells and in lower levels on monocytes, granulocytes and platelets.
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Available Conjugates
This antibody is also available conjugated to FITC and biotin. For flow cytometry use 5-10µl/106 cells.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
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Purification Method
Protein 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 :
BMP8B AntibodyDescription:
Bone Morphogenetic protein-8b, Mouse Anti Human
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
Product # :
ANT-558Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.
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Synonyms
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human BMP8B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human BMP8B protein 264-402 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and k light chain.
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Clone
PAT13E6AT.
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Applications
BMP8B antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
BMP8B antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
D-Dimer HumanDescription:
D-Dimer Human
Product # :
PRO-2795Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
D-Dimer Human produced in Human Plasma is a specific degradation product of cross-linked fibrin and is used as a marker of hypercoagulation state that causes cardio-vascular diseases. D-Dimer is purified by proprietary chromatographic technique.
Source
Human plasma.
Formulation
D-Dimer was lyophilized from 10mM Tris-HCl and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized D-Dimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution D-Dimer 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 D-Dimer in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
D-dimer, a small protein fragment present in the blood after a blood clot dissolves, is a vital marker in the realms of hematology and vascular medicine. Its presence signifies the ongoing process of fibrinolysis, where clots formed in blood vessels are broken down. Beyond its diagnostic significance, understanding the roles of D-dimer in human physiology and pathology is essential for comprehending coagulation disorders and cardiovascular diseases. This research delves into the multifaceted aspects of D-dimer, exploring its physiological functions, diagnostic applications, and implications in various medical conditions.
Physiological Functions:
In physiological conditions, coagulation and fibrinolysis are finely regulated processes, ensuring hemostasis and preventing excessive bleeding or clot formation. D-dimer is a natural byproduct of fibrinolysis, created when plasmin, an enzyme, breaks down fibrin clots. In this context, D-dimer acts as a marker of the body's intricate balance between clot formation and dissolution. It reflects the ongoing maintenance of vascular integrity, showcasing the body's ability to prevent unnecessary clotting.
Diagnostic Significance:
D-dimer holds significant diagnostic value, especially in the context of thrombotic disorders. Elevated levels of D-dimer in the blood are indicative of increased fibrinolysis, potentially signaling an underlying clotting disorder. Clinically, D-dimer assays are widely used to rule out thromboembolic events, such as deep vein thrombosis (DVT) or pulmonary embolism (PE). Moreover, D-dimer levels are crucial in risk stratification and decision-making processes in emergency departments, aiding in the timely diagnosis and treatment of thrombotic conditions.
Cardiovascular Implications:
Research has indicated a strong correlation between elevated D-dimer levels and cardiovascular diseases. In conditions like coronary artery disease (CAD) and stroke, where abnormal clot formation contributes to pathogenesis, D-dimer serves as a prognostic marker. Its presence hints at the ongoing vascular damage and the potential risk of acute events. Studying these correlations provides valuable insights into the progression of cardiovascular diseases, aiding in the development of targeted therapeutic strategies.
Beyond Coagulation Disorders:
Interestingly, recent research has begun to explore D-dimer's involvement in conditions beyond coagulation disorders. Studies suggest links between elevated D-dimer levels and inflammatory diseases, such as sepsis and rheumatoid arthritis. This expanding scope highlights the intricate interplay between coagulation, inflammation, and immune responses, shedding light on novel avenues for therapeutic interventions.
Conclusion:
D-dimer, once a simple marker of fibrinolysis, has evolved into a multifaceted indicator in the realm of medicine. Its physiological role as a byproduct of clot dissolution is intertwined with its diagnostic significance in thrombotic events and cardiovascular diseases. Furthermore, emerging research is uncovering its involvement in inflammatory processes, broadening its clinical implications. By delving into the complexities of D-dimer, scientists and clinicians pave the way for a deeper understanding of coagulation disorders and associated conditions, driving advancements in diagnostics and therapies.
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 RatDescription:
Vascular Endothelial Growth Factor Rat Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-392Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor Rat Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38,750 Dalton. The VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 10mM NaP, pH 7.5.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 4.0-8.0 ng/ml.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/ macrophagemigration, 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 mitogenesisand 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 are 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 White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vascular Endothelial Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF 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 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
MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.
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 :
PGF1 MouseDescription:
Placental Growth Factor-1 Mouse Recombinant
Placenta growth factor, PlGF, PGF1.
Product # :
CYT-907Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PGF1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 138 amino acids (27-158a.a.) and having a molecular mass of 15.9kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). PGF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PGF1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 0.1mM PMSF and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Placental Growth Factor, also known as PGF is rich in trophoblastic giant cells which are linked with the parietal yolk sac at early stages of embryogenesis. Furthermore, the secretion of PGF by trophoblastic giant cells is the signal which initiates as well as co-ordinates vascularization in the deciduum and placenta during early embryogenesis.
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Synonyms
Placenta growth factor, PlGF, PGF1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
AGNNSTEVEV VPFNEVWGRS YCRPMEKLVY ILDEYPDEVS HIFSPSCVLL SRCSGCCGDE GLHCVPIKTA NITMQILKIP PNRDPHFYVE MTFSQDVLCE CRPILETTKA ERRKTKGKRK RSRNSQTEEP HPHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin tA OvineDescription:
Leptin Antagonist Triple Mutant Ovine Recombinant
Product # :
CYT-356Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin 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-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, 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 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB1 Human RecombinantDescription:
Transforming Growth Factor-Beta 1 Human Recombinant
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Product # :
CYT-716Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFB1 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa. The TGFB1 is purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA) And trehalose (1:20 protein to Trehalose ratio).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is 0.142ng/ml, corresponding to a specific activity of 7.4x106units/mg.
More Info
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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human 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 TGFB1 in sterile 10mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
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Background
Title: Transforming Growth Factor-Beta 1 Human Recombinant: A Promising Tool for Biomedical Research
Abstract:
Transforming Growth Factor-Beta 1 (TGF-β1) is a crucial cytokine involved in diverse cellular processes. This research paper provides an in-depth analysis of human recombinant TGF-β1, focusing on its production, purification, and applications in biomedical research. The paper discusses the significance of TGF-β1 in tissue engineering, regenerative medicine, and immunology. Furthermore, it elucidates the potential therapeutic implications of recombinant TGF-β1 in various diseases and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of TGF-β1 and its utility as a research tool in biomedical sciences.Introduction:
Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that regulates cellular processes such as cell growth, differentiation, and immune modulation. Human recombinant TGF-β1 is synthesized using genetic engineering techniques, enabling the production of large quantities of biologically active protein for research purposes.Production and Purification:
Recombinant TGF-β1 is typically produced in expression systems such as bacteria, yeast, or mammalian cells. The protein is then purified using various chromatographic techniques to obtain a highly pure and active form. Quality control measures ensure the biological activity and integrity of the recombinant protein.Biomedical Applications:
Human recombinant TGF-β1 has found broad applications in biomedical research. In tissue engineering and regenerative medicine, it plays a critical role in promoting cell proliferation, extracellular matrix production, and tissue repair. TGF-β1 is also involved in immune modulation, influencing immune cell differentiation and function. Recombinant TGF-β1 is a valuable tool for studying these processes and developing therapeutic interventions.Therapeutic Implications:
The dysregulation of TGF-β1 signaling is associated with various diseases, including fibrosis, cancer, and autoimmune disorders. Recombinant TGF-β1 offers potential therapeutic applications through its ability to modulate cellular responses. Ongoing research aims to develop targeted therapies that specifically regulate TGF-β1 signaling for the treatment of these conditions.Conclusion:
Human recombinant TGF-β1 holds immense potential as a research tool in biomedical sciences. Its production, purification, and applications in tissue engineering, regenerative medicine, and immunology contribute to advancing our understanding of cellular processes and disease mechanisms. With ongoing research, recombinant TGF-β1 may pave the way for novel therapeutic strategies in various medical fields.
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 :
TGFA HumanDescription:
Transforming Growth Factor-Alpha Human Recombinant
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
Product # :
CYT-871Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.
More Info
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Introduction
Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.
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Synonyms
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFA 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 TGFA 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
VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.
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Background
Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications
Abstract:
Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.Introduction:
TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.Production Process and Characteristics:
TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.Therapeutic Applications:
TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.Advantages and Challenges:
The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.Conclusion:
TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.
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 :
Visfatin MouseDescription:
Visfatin Mouse Recombinant
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
CYT-447Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Visfatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-491) containing a 20 aa His tag and having 511 amino acids. The total molecular mass is 57kDa. The Visfatin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 1x PBS pH-7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-?, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes. -
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Physical Appearance
Sterile Filtered colorless 1mg/ml 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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECREKKTENSKVR KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERGWNYILEKYDG HLPIEVKAVP EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPITVATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGHDLLHTVFKNGKVTKS YSFDEVRKNA QLNIEQDVAP H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
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
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.
- View Data Sheet
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 :
Quantity :
Shipping Method :
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.
-
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.
- View Data Sheet
Name :
CTSF HumanDescription:
Cathepsin-F Human Recombinant
800x600 CATSF, CLN13, Cathepsin F, EC=3.4.22.41. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}
Product # :
ENZ-738Price :
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Description
800x600 CTSF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (271-484) and having a molecular mass of 26kDa.CTSF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSF solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin F ( CTSF) is a member of the peptidase C1 family. Cathepsins are papain familycysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.
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Synonyms
CATSF, CLN13, Cathepsin F, EC=3.4.22.41.
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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 MGSAPPEWDW RSKGAVTKVK DQGMCGSCWA FSVTGNVEGQ WFLNQGTLLS LSEQELLDCD KMDKACMGGL PSNAYSAIKN LGGLETEDDY SYQGHMQSCN FSAEKAKVYI NDSVELSQNE QKLAAWLAKR GPISVAINAF GMQFYRHGIS RPLRPLCSPW LIDHAVLLVG YGNRSDVPFW AIKNSWGTDW GEKGYYYLHR GSGACGVNTM ASSAVVD.
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 :
SCF Human, HEKDescription:
Stem Cell Factor Human Recombinant, HEK
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-111Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SCF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 35-45kDa due to glycosylation.The SCF is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
SCF was lyophilized from a 0.2µm filtered solution (1mg/ml) containing 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line).
The EC50 is 15.25ng/ml.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 SCF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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 :
MCP 1 AntibodyDescription:
Macrophage/Monocyte Chemotactic & Activating Factor, Mouse Anti-Human
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Product # :
ANT-119Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Formulation
1mg/ml in PBS (after reconstitution) Shipping ConditionsAntibody is shipped lyophilized at ambient temperature.
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Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
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Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human MCAF.
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Ig Subclass
Mouse IgG2a.
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Clone
YNR-HMCAF.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation.
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Note
MCAF does not bind to plastic as good as most proteins - use higher concentration for proper binding.
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Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson Laboratories) 1:5,000 dilution will give 0.3 O.D within 10 minutes.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
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Purification Method
Ion exchange.
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 :
TNNI1 AntibodyDescription:
Troponin I Type 1, Mouse Anti Human
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
Product # :
ANT-474Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.01% Sodium Azide.
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Introduction
Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.
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Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human TNNI1 mAb, clone PAT36E7A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human TNNI1 protein.
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Ig Subclass
Mouse IgG2b heavy chain and Kappa light chain.
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Clone
PAT36E7A.
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Applications
The antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:5000. Recommended starting dilution is 1:5000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
TNNI1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
TNFRSF4 HumanDescription:
TNF Receptor Superfamily Member 4 Human Recombinant
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
Product # :
CYT-1039Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 425 amino acids (29-214a.a.) and having a molecular mass of 46.9Da. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF4 is expressed with a 239 amino acid higG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with mouse OX40 Ligand/TNFSF4 The ED50 range ≤ 0.15 ug/ml.
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Introduction
TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.
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Synonyms
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
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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
LHCVGDTYPS NDRCCHECRP GNGMVSRCSR SQNTVCRPCG PGFYNDVVSS KPCKPCTWCN LRSGSERKQL CTATQDTVCR CRAGTQPLDS YKPGVDCAPC PPGHFSPGDN QACKPWTNCT LAGKHTLQPA SNSSDAICED RDPPATQPQE TQGPPARPIT VQPTEAWPRT SQGPSTRPVE VPGGRALEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ABI3 HumanDescription:
ABI Family, Member 3 Human Recombinant
ABI Family Member 3, ABI Gene Family Member 3, New Molecule Including SH3, SSH3BP3, NESH.
Product # :
PRO-1227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ABI3 Human Recombinant produced in E. coli is a single polypeptide chain containing 389 amino acids (1-366) and having a molecular mass of 41.4 kDa.ABI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ABI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ABI gene family member 3 (ABI3) is a member of the ABI family. Members of the ABI family encode proteins which contain a homeobox homology domain, proline rich region and Src-homology 3 (SH3) domain. Abi family members are assumed to negatively regulate cell growth and transformation, including cellular transformation through v-Abl as well controlling as mediate cell motility by regulating actin polymerization in lamellipodia and filopodia. ABI3 impedes ectopic metastasis of tumor cells as well as cell migration, which is accomplished through interaction with p21-activated kinase.
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Synonyms
ABI Family Member 3, ABI Gene Family Member 3, New Molecule Including SH3, SSH3BP3, NESH.
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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 MGSMAELQQL QEFEIPTGRE ALRGNHSALL RVADYCEDNY VQATDKRKAL EETMAFTTQA LASVAYQVGN LAGHTLRMLD LQGAALRQVE ARVSTLGQMV NMHMEKVARR EIGTLATVQR LPPGQKVIAP ENLPPLTPYC RRPLNFGCLD DIGHGIKDLS TQLSRTGTLS RKSIKAPATP ASATLGRPPR IPEPVHLPVV PDGRLSAASS ASSLASAGSA EGVGGAPTPK GQAAPPAPPL PSSLDPPPPP AAVEVFQRPP TLEELSPPPP DEELPLPLDL PPPPPLDGDE LGLPPPPPGF GPDEPSWVPA SYLEKVVTLY PYTSQKDNEL SFSEGTVICV TRRYSDGWCE GVSSEGTGFF PGNYVEPSC
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.