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1000 results found for “Cytokeratin”
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Name :
CLTB HumanDescription:
Clathrin, Light Chain B Human Recombinant
Clathrin light chain B, Lcb, CLTB.
Product # :
PRO-1172Price :
Quantity :
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Shipped with Ice Packs
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Description
CLTB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211 a.a) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear higher).CLTB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLTB protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 0.2mM PMSF and 100mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Clathrin light chain B (CLTB) is a member of the clathrin light chain family. Clathrin is a protein that has a key role in the formation of coated vesicles. CLTB functions as the key structural component of the lattice-type cytoplasmic face of coated pits and vesicles which capture certain macromolecules during receptor-mediated endocytosis. CLTB forms a triskelion form comprised of 3 clathrin heavy chains and 3 light chains. When the triskelia interact they form a polyhedral pattern which encircles the vesicle. CME (Clathrin-mediated endocytosis) controls numerous cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission.
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Synonyms
Clathrin light chain B, Lcb, CLTB.
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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 MGSMADDFGF FSSSESGAPE AAEEDPAAAF LAQQESEIAG IENDEGFGAP AGSHAAPAQP GPTSGAGSED MGTTVNGDVF QEANGPADGY AAIAQADRLT QEPESIRKWR EEQRKRLQEL DAASKVTEQE WREKAKKDLE EWNQRQSEQV EKNKINNRAS
EEAFVKESKE ETPGTEWEKV AQLCDFNPKS SKQCKDVSRL RSVLMSLKQT PLSR.
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 :
VAMP3 HumanDescription:
Synaptobrevin-3 Human Recombinant
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Product # :
PRO-652Price :
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Shipped with Ice Packs
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Description
VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.
Source
Escherichia Coli.
Formulation
The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
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Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
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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
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.
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 :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
Quantity :
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Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Omentin 298 a.a. HumanDescription:
Omentin 298 a.a. Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-061Price :
Quantity :
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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.
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Name :
Periostin HumanDescription:
Periostin Human Recombinant
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Product # :
CYT-452Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The OSF2 His-Tagged Fusion Protein Human is produced in E. coli, and its molecular weight is 75 kDa protein containing 648 amino acid residues of the human OSF-2 and 23 additional amino acid residues - HisTag, Xa - cleavage site.
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart. -
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. 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
MGHHHHHHHH HHSSGHIEGR HMRNNHYDKI LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS TCKNWYKKSI CGQKTTVLYE CCPGYMRMEG MKGCPAVLPI DHVYGTLGIV GATTTQRYSD ASKLREEIEG KGSFTYFAPS NEAWDNLDSD IRRGLESNVN VELLNALHSH MINKRMLTKD LKNGMIIPSM YNNLGLFINH YPNGVVTVNC ARIIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFIEAEDDLS SFRAAAITSD ILEALGRDGH FTLFAPTNEA FEKLPRGVLE RFMGDKVASEALMKYHILNT LQCSESIMGG AVFETLEGNT IEIGCDGDSI TVNGIKMVNK KDIVTNNGVI HLIDQVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASALR PDGEYTLLAP VNNAFSDDTL SMVQRLLKLI LQNHILKVKV GLNELYNGQI LETIGGKQLR VFVYRTAVCI ENSCMEKGSK QGRNGAIHIF REIIKPAEKS LHEKLKQDKR FSTFLSLLEA ADLKELLTQP GDWTLFVPTN DAFKGMTSEE KEILIRDKNA LQNIILYHLT PGVFIGKGFE PGVTNILKTT QGSKIFLKEV NDTLLVNELK SKESDIMTTN GVIHVVDKLL YPADTPVGND QLLEILNKLI KYIQIKFVRG STFKEIPVTV Y.
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 :
CAMP HumanDescription:
Cathelicidin Antimicrobial Peptide Human Recombinant
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Product # :
PRO-1405Price :
Quantity :
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Shipped with Ice Packs
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Description
CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
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Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.
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 :
CDH5 MouseDescription:
Cadherin 5 Mouse Recombinant
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
Product # :
PRO-2244Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDH5 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 583 amino acids (25-599a.a.) and having a molecular mass of 66.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH5 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CDH5 protein solution (0.5mg/ml) contains 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
Cadherin-5, also known as CDH5 is a classical cadherin which belongs to the cadherin superfamily. The CDH5is located in a six-cadherin cluster in a region on the long arm of chromosome 16 which is involved in loss ofheterozygosity events in breast as well as prostate cancer. CDH5 is a calcium-dependent cell-celladhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highlyconserved cytoplasmic tail. Furthermore, CDH5 functions as a classic cadherin by passing on to cells the ability to adhere in ahomophilic manner, CDH5 plays a significant role in endothelial cell biology through control of the cohesion as well as organization of the intercellular junctions.
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Synonyms
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
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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
GPNFPQIDTP NMLPAHHRQK RDWIWNQMHI DEEKNESLPH YVGKIKSNVN RQNAKYVLQG EFAGKIFGVD ANTGNVLAYE RLDREKVSEY FLTALIVDKN TNKNLEQPSS FTVKVHDIND NWPVFSHQVF NASVPEMSAI GTSVIRVTAV DADDPTVAGH ATVLYQIVKG NEYFSIDNSG LIFTKIKNLD REKQAEYKIV VETQDALGLR GESGTATVMI RLEDINDNFP VFTQSTYTFS VPEDIRVGKP LGFLTVVDPD EPQNRMTKYS IMQGEYRDTF TIETDPKRNE GIIKPTKSLD YEVIQQYTFY IEATDPTIRY EYLSSTSGKN KAMVTINVLD VDEPPVFQRH FYHFKLPENQ KKPLIGTVVA KDPDKAQRSI GYSIRKTSDR GQFFRITKQG NIYNEKELDR ETYAWYNLTV EANELDSRGN PVGKESIVQV YIEVLDENDN PPEFAQPYEP KVCENAAQGK LVVQISATDK DVVPVNPKFK FALKNEDSNF TLINNHDNTA NITVKYGQFN REHAKFHYLP VLISDNGVPS LTGTSTLTVG VCKCNEQGEF TFCEEMAAQA GVSIQLEHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CKMT3 HumanDescription:
Creatine Kinase Muscle Type-3 Human Recombinant
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.
Product # :
CKI-272Price :
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Shipped with Ice Packs
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Description
CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Synonyms
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent 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 :
CXCL3 Rat alphaDescription:
GRO-Gamma Rat Recombinant (CXCL3), CINC-2 alpha
Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.
Product # :
CHM-258Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO-g Rat Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Rat CXCL3 lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GRO-gamma in sterile 18Mcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.
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Background
What is the molecular weight/Mw of CXCL3 RAT ALPHA Protein?
CXCL3 RAT ALPHA Protein has a total Mw of 7.8kDa.
What is the source or expression system of CXCL3 RAT ALPHA Protein?
Escherichia Coli.
What is the Purity of CXCL3 RAT ALPHA Protein?
CXCL3 RAT ALPHA Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 RAT ALPHA Protein?
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.
What is the amino acid sequence of CXCL3 RAT ALPHA Protein?
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.
What applications can CXCL3 RAT ALPHA Protein be used in?
CXCL3 RAT ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 RAT ALPHA Protein?
The endotoxin level is minimal, CXCL3 RAT ALPHA 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 :
BMP 4 HumanDescription:
Bone Morphogenetic Protein-4 Human Recombinant
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-361Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
-
Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
-
Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.
What is the source or expression system of BMP4 Protein?
Escherichia Coli.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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 :
CKMB1 HumanDescription:
Creatine Kinase MB Isoenzyme Type-1 Human Recombinant
Creatine Kinase MB 1, CKMB1
Product # :
CKI-269Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CKMB1 Human Recombinant produced in E.Coli is a non covalently linked heterodimer that consists of 381 a.a. and having a total Mw of ~85.6kDa. The CKMB1 is purified by proprietary chromatographic techniques.
Source
E.Coli
Formulation
CKMB1 was lyophilized a concentrated solution containing 20mM Tris, 150mM NaCl, pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
CKMB1 activity was measured kinetically by the CK-NAC assay at 37°C which was found to be between 500-600 units/mg. 1U converts 1µmole of creatine phosphate to creatine/min at 37˚CMore Info
-
Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
-
Synonyms
Creatine Kinase MB Isoenzyme Type-1, CK MB1
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized CKMB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CKMB1 in sterile 18MΩ-cm H2O at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
CKM1
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQCKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
-
Background
What is the molecular weight / Mw of CKMB1 Protein?
CKMB1 Protein is a non covalently heterodimer having a total Mw of 85.6
What is the source or expression system of CKMB1 Protein?
Escherichia Coli.
What is the Purity of CKMB1 Protein?
CKMB1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CKMB1 Protein?
The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.
What is the amino acid sequence of CKMB1 Protein?
CKM1
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
What applications can CKMB1 Protein be used in?
CKMB1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CKMB1 Protein?
The endotoxin level is minimal, CKMB1 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 :
Midkine HumanDescription:
Midkine Human Recombinant
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
Product # :
CYT-192Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.More Info
-
Introduction
Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis. -
Synonyms
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Midkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Midkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.
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 :
ITAC (63-87) HumanDescription:
ITAC (63-87 a.a.) Human Recombinant
ITAC, I-TAC, CXCL-11, CXCL11.
Product # :
CHM-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Synonyms
ITAC, I-TAC, CXCL-11, CXCL11.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized I-TAC at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Background
I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10.
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 :
G CSF AntibodyDescription:
Granulocyte Colony Stimulating Factor, Mouse Anti-Human
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
ANT-184Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
-
Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene.
Granulocyte/macrophage colony-stimulating factors are cytokines that act 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. -
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
-
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.Human G-CSF.
-
Ig Subclass
Mouse IgG.
-
Clone
NYRhGCSF.
-
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
-
Titer
By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
-
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.
-
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.
- View Data Sheet
Name :
CNTF RatDescription:
Ciliary Neurotrophic Factor Rat Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-654Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CNTF Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22834 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.025% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.More Info
-
Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CNTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CNTF in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
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Amino Acid Sequence
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH
YGAKDKQM. -
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.
What is the amino acid sequence of CNTF Protein?
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH YGAKDKQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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 :
Chitinase ProteinDescription:
Chitinase Clostridium Paraputrificum Recombinant
Product # :
ENZ-031Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. The Chitinase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Chitinase lyophilized from a 0.2µm filtered concentrated solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Chitinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Chitinase should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Chitinase in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.
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 AntibodyDescription:
Omentin, Mouse Anti Human
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
ANT-505Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
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
-
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human Omentin mAb, clone PAT6C11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human Omentin protein 17-313 amino acids purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and Kappa light chain.
-
Clone
PAT6C11AT.
-
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 starting dilution is 1:250.
-
Type
Mouse Anti Human Monoclonal.
-
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.
-
Purification Method
Omentin antibody was purified 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 :
CSK HumanDescription:
C-Src Tyrosine Kinase Human Recombinant
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
Product # :
PKA-062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
CSK Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 53.1 kDa.The CSK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSK protein (0.5mg/ml) is containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.
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Synonyms
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
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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 MGSMSAIQAA WPSGTECIAK YNFHGTAEQD LPFCKGDVLT IVAVTKDPNW YKAKNKVGRE GIIPANYVQK REGVKAGTKL SLMPWFHGKI TREQAERLLY PPETGLFLVR ESTNYPGDYT LCVSCDGKVE HYRIMYHASK LSIDEEVYFE NLMQLVEHYT SDADGLCTRL IKPKVMEGTV AAQDEFYRSG WALNMKELKL LQTIGKGEFG DVMLGDYRGN KVAVKCIKND ATAQAFLAEA SVMTQLRHSN LVQLLGVIVE EKGGLYIVTE YMAKGSLVDY LRSRGRSVLG GDCLLKFSLD VCEAMEYLEG NNFVHRDLAA RNVLVSEDNV AKVSDFGLTK EASSTQDTGK LPVKWTAPEA LREKKFSTKS DVWSFGILLW EIYSFGRVPY PRIPLKDVVP RVEKGYKMDA PDGCPPAVYE VMKNCWHLDA AMRPSFLQLR EQLEHIKTHE LHL.
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 :
CTHRC1 Human, HEKDescription:
Collagen Triple Helix Repeat Containing 1 Human Recombinant, HEK
Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.
Product # :
PRO-2028Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CTHRC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser31-Lys243) containing a total of 219 amino acids, having a calculated molecular mass of 23.9kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
CTHRC1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.
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Synonyms
Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CTHRC1 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
SEIPKGKQKA QLRQREVVDL YNGMCLQGPA GVPGRDGSPG ANGIPGTPGI PGRDGFKGEK GECLRESFEE SWTPNYKQCS WSSLNYGIDL GKIAECTFTK MRSNSALRVL FSGSLRLKCR NACCQRWYFT FNGAECSGPL PIEAIIYLDQ GSPEMNSTIN IHRTSSVEGL CEGIGAGLVD VAIWVGTCSD YPKGDASTGW NSVSRIIIEE LPK HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARMC10 HumanDescription:
Armadillo Repeat Containing 10 Human Recombinant
Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.
Product # :
PRO-1453Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.
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Synonyms
Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.
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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 MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.
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 :
SOST Human, HEKDescription:
Sclerostin Human Recombinant, HEK
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-2481Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).
Source
HEK293 Cells.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SOST 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
QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
STK11 HumanDescription:
Serine/Threonine Kinase 11 Human Recombinant
Serine/threonine-protein kinase STK11, Liver kinase B1, LKB1, hLKB1, Renal carcinoma antigen NY-REN-19, STK11, LKB1, PJS
Product # :
PKA-123Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-433) and having a molecular mass of 51kDa.STK11 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The STK11 solution (0.5mg/ml) contains 10% Glycerol and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STK11, which controls cell polarity and functions as a tumour suppressor, belongs to the serine/threonine kinase family. Mutations in this gene have been linked to Peutz-Jeghers syndrome- an autosomal dominant disorder. It is characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms.
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Synonyms
Serine/threonine-protein kinase STK11, Liver kinase B1, LKB1, hLKB1, Renal carcinoma antigen NY-REN-19, STK11, LKB1, PJS
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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 MGSMEVVDPQ QLGMFTEGEL MSVGMDTFIH RIDSTEVIYQ PRRKRAKLIG KYLMGDLLGE GSYGKVKEVL DSETLCRRAV KILKKKKLRR IPNGEANVKK EIQLLRRLRH KNVIQLVDVL YNEEKQKMYM VMEYCVCGMQ EMLDSVPEKR FPVCQAHGYF CQLIDGLEYL HSQGIVHKDI KPGNLLLTTG GTLKISDLGV AEALHPFAAD DTCRTSQGSP AFQPPEIANG LDTFSGFKVD IWSAGVTLYN ITTGLYPFEG DNIYKLFENI GKGSYAIPGD CGPPLSDLLK GMLEYEPAKR FSIRQIRQHS WFRKKHPPAE APVPIPPSPD TKDRWRSMTV VPYLEDLHGA DEDEDLFDIE DDIIYTQDFT VPGQVPEEEA SHNGQRRGLP KAVCMNGTEA AQLSTKSRAE GRAPNPARKA CSASSKIRRL SACKQQ
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 :
CDK3 HumanDescription:
Cyclin-Dependent Kinase 3 Human Recombinant
Cyclin-dependent kinase 3, Cell division protein kinase 3, CDK3, CDKN3.
Product # :
PKA-055Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDK3 Human Recombinant produced in E. coli is a single polypeptide chain containing 328 amino acids (1-305) and having a molecular mass of 37.4kDa.CDK3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDK3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cyclin-dependent kinase 3, also known as CDK3, is a part of the cyclin-dependent protein kinase family. CDK3 promotes entry into S phase, partially by activating members of the E2F family of transcription factors. CDK3 also associates with cyclin C and phosphorylates the retinoblastoma one protein to promote exit from G0.
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Synonyms
Cyclin-dependent kinase 3, Cell division protein kinase 3, CDK3, CDKN3.
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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 MGSMDMFQKV EKIGEGTYGV VYKAKNRETG QLVALKKIRL DLEMEGVPST AIREISLLKE LKHPNIVRLL DVVHNERKLY LVFEFLSQDL KKYMDSTPGS ELPLHLIKSY LFQLLQGVSF CHSHRVIHRD LKPQNLLINE LGAIKLADFG LARAFGVPLR TYTHEVVTLW YRAPEILLGS KFYTTAVDIW SIGCIFAEMV TRKALFPGDS EIDQLFRIFR MLGTPSEDTW PGVTQLPDYK GSFPKWTRKG LEEIVPNLEP EGRDLLMQLL QYDPSQRITA KTALAHPYFS SPEPSPAARQ YVLQRFRH.
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 :
CRISP1 HumanDescription:
Cysteine-Rich Secretory Protein 1 Human Recombinant
Cysteine-rich secretory protein 1, ARP, CRISP-1, AEGL1, Acidic epididymal glycoprotein-like 1, HSCRISP1D, HSCRISP1G, HUMARP, AEG-like protein, cysteine-rich secretory protein-1 delta.
Product # :
PRO-473Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The CRISP1 Protein Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (Lys 22 - Lys 249) having a molecular mass of 27kDa.CRISP1 is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.5mg/ml solution containing 20mM TRIS, 50mM NaCl, pH 7.5.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Insemination involves of a series of specific cell-cell interactions concluding in the fusion of the sperm and egg plasma membranes. Recognition, binding, and fusion take place through the interface of complementary molecules which are localized to specific domains of the sperm and egg plasma membranes. In the sperm, the postacrosomal region or equatorial segment is involved in sperm-egg plasma membrane fusion. The protein encoded by this gene belongs to the cysteine-rich secretory protein (CRISP) family. CRISP1 is expressed in the epididymis, is secreted into the epididymal lumen, and binds to the postacrosomal region of the sperm head, where it takes part in sperm-egg fusion.
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Synonyms
Cysteine-rich secretory protein 1, ARP, CRISP-1, AEGL1, Acidic epididymal glycoprotein-like 1, HSCRISP1D, HSCRISP1G, HUMARP, AEG-like protein, cysteine-rich secretory protein-1 delta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CRISP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CRISP1 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 CRISP1 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
MKHHHHHHAS KKKSARDQFN KLVTDLPNVQ EEIVNIHNAL RRRVVPPASN MLKMSWSEEA AQNARIFSKY CDMTESNPLE RRLPNTFCGE NMHMTSYPVS WSSVIGVWYS ESTSFKHGEW TTTDDDITTD HYTQIVWATS YLIGCAIASC RQQGSPRYLY VCHYCHEGND PETKNEPYKT GVPCEACPSN CEDKLCTNPC IYYDEYFDCD IQVHYLGCNH STTILFCKAT CLCDTEIK
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Applications
Western blotting, ELISA.
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.