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1000 results found for “Prohibitin”
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Name :
MYL9 HumanDescription:
Myosin Light Chain 9 Human Recombinant
Myosin regulatory light polypeptide 9, 20 kDa myosin light chain, LC20, MLC-2C, Myosin RLC, Myosin regulatory light chain 2, smooth muscle isoform, Myosin regulatory light chain 9, Myosin regulatory light chain MRLC1, MYL9, MLC2, MRLC1, MYRL2, MGC3505.
Product # :
PRO-107Price :
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Shipped with Ice Packs
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Description
MYL9 Human Recombinant fused with a20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing192 amino acids (1-172 a.a.) and having a molecular mass of 21.9kDa. The MYL9 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MYL9 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MYL9 is one of the numerous regulatory myosin light chains. Myosin which is a structural component of the muscle consists of 2 heavy chains and 4 light chains. MYL9 is a myosin light chain regulates muscle contraction by modulating the ATPase activity of myosin heads. MYL9 binds calcium and is activated by myosin light chain kinase. Regulatory myosin light chains regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of regulatory myosin light chains is catalyzed by MLCK in the presence of calcium and calmodulin and it increases the actin-activated myosin ATPase activity, thus regulates the contractile activity.
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Synonyms
Myosin regulatory light polypeptide 9, 20 kDa myosin light chain, LC20, MLC-2C, Myosin RLC, Myosin regulatory light chain 2, smooth muscle isoform, Myosin regulatory light chain 9, Myosin regulatory light chain MRLC1, MYL9, MLC2, MRLC1, MYRL2, MGC3505.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD.
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 :
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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 :
OTC HumanDescription:
Ornithine Carbamoyltransferase Human Recombinant
Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.
Product # :
ENZ-596Price :
Quantity :
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Shipped with Ice Packs
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Description
OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.
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Synonyms
Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.
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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 MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.
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 :
IL 7 Human, YeastDescription:
Interleukin-7 Human Recombinant, Yeast
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-298Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.More Info
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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin -7 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 Asp-Cys-Asp-Ile-Glu.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.418 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-7 as a Reference Standard.
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 :
BTLA HumanDescription:
B And T Lymphocyte Associated Human Recombinant
B- and T-lymphocyte attenuator, B- and T-lymphocyte-associated protein, CD272, B And T Lymphocyte Associated, B- And T-Lymphocyte-Associated Protein, B- And T, Lymphocyte Attenuator, CD272 Antigen, BTLA1.
Product # :
PRO-2505Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BTLA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 136 amino acids (31-157 a.a.) and having a molecular mass of 15.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).BTLA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
BTLA 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.
More Info
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Introduction
BTLA, also known as B And T Lymphocyte Associated, is an inhibitory molecule which is part of the Ig superfamily. BTLA is a type 1 transmembrane glycoprotein in the CD28 family of T cell costimulatory molecules. BTLA is a 3rd inhibitory receptor on T lymphocytes with resemblances to CTLA-4 & PD-1. Moreover, BTLA is a ligand for TNF (receptor) superfamily, TNFRSF14, and HVEM. BTLA-HVEM complexes negatively regulate T-cell immune responses.
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Synonyms
B- and T-lymphocyte attenuator, B- and T-lymphocyte-associated protein, CD272, B And T Lymphocyte Associated, B- And T-Lymphocyte-Associated Protein, B- And T, Lymphocyte Attenuator, CD272 Antigen, BTLA1.
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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
ADPKESCDVQ LYIKRQSEHS ILAGDPFELE CPVKYCANRP HVTWCKLNGT TCVKLEDRQT SWKEEKNISF FILHFEPVLP NDNGSYRCSA NFQSNLIESH STTLYVTDVK SASERPSKDE MASRPWLLYS 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 :
C10ORF54 HumanDescription:
Chromosome 10 Open Reading Frame 54 Human Recombinant
C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.
Product # :
PRO-2259Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
C10ORF54 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (33-194 a.a) and having a molecular mass of 19.1kDa. (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). C10ORF54 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
C10ORF54 protein solution (0.5mg/ml) containing 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
Chromosome 10 Open Reading Frame 54, also known as C10ORF54 is part of the immunoglobulin superfamily. Like a transmembrane molecule, C10ORF54 is expressed in the bone on embryonic stem cells (ESCs), and on tumor cell surface as well. Accordingly, C10ORF54 supports the differentiation of ESC and ehhances BMP4 induced signaling in ESC, however C10ORF54 is also down regulated following to BMP4 exposure.
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Synonyms
C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.
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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
FKVATPYSLY VCPEGQNVTL TCRLLGPVDK GHDVTFYKTW YRSSRGEVQT CSERRPIRNL TFQDLHLHHG GHQAANTSHD LAQRHGLESA SDHHGNFSIT MRNLTLLDSG LYCCLVVEIR HHHSEHRVHG AMELQVQTGK DAPSNCVVYP SSSQDSENIT AAVEHHHHHH.
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 :
FKBP2 HumanDescription:
FK506 Binding Protein 2 Human Recombinant
FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.
Product # :
ENZ-503Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FKBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (22-142 a.a.) and having a molecular mass of 13.4 kDa. The FKBP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FKBP2 solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 270 nmoles/min/ug, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
FKBP2 is part of the immunophilin protein family, which takes part in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP2 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. FKBP2 functions as an ER chaperone and as a component of membrane cytoskeletal scaffolds.
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Synonyms
FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.
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Physical Appearance
Sterile Filtered clear 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
MATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK IPGGATLVFE VELLKIERRT EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CX3CL1 Human, HisDescription:
Fractalkine Human Recombinant (CX3CL1), His Tag
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-360Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
Fractalkine Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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Physical Appearance
Sterile Filtered 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 MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
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Background
What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.
What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
What applications can CX3CL1 HUMAN, HIS Protein be used in?
CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TPRKB HumanDescription:
TP53RK Binding Protein Human Recombinant
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
Product # :
PRO-1185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.
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Synonyms
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
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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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GHBP HumanDescription:
GHBP Human Recombinant
Product # :
CYT-238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GHBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids and having a molecular mass of 28107.01 Dalton. GHR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GHBP was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
GHBP is fully biologically active as evidenced by its ability of forming 2:1 complex with G.H.
More Info
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Introduction
GHBP is a transmembrane receptor for GH. Binding of GH to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the GH insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GHBP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP 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 GHBP 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
AFSGSEATAAILSRAPWSLQSVNPGLKTNS SKEPKFTKCRSPERETFSCHWTDEVHHGTK
NLGPIQLFYTRRNTQEWTQEWKECPDYVSA GENSCYFNSSFTSIWIPYCIKLTSNGGTVD
EKCFSVDEIVQPDPPIALNWTLLNVSLTGI HADIQVRWEAPRNADIQKGWMVLEYELQYK
EVNETKWKMMDPILTTSVPVYSLKVDKEYE VRVRSKQRNSGNYGEFSEVLYVTLPQMSQF
TCEEDFYF. -
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GHBP as a Reference Standard.
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 :
CHGB HumanDescription:
Chromogranin B Human Recombinant
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
Product # :
PRO-824Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
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Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
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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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.
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 :
MAPT Human 383a.a.Description:
Microtubule-Associated Protein Tau 383 a.a. Human Recombinant
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-012Price :
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Description
MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.
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 :
IL 1RA Human HisDescription:
Interleukin-1 Receptor Antagonist Human Recombinant, His Tag
IRAP, IL1F3, IL1RA; IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
CYT-481Price :
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Description
IL1Ra Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 152 amino acids fragment (26-177) and having a total molecular mass of 21.63kDa with an amino-terminal hexahistidine tag. The IL-1Ra His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-1Ra His-tag protein is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IL-1Ra is the natural antagonist of the pro-inflammatory cytokines Interleukin-1? and Interleukin-1?. IL-1Ra is produced by a variety of cells including monocytes, macrophages, neutrophils and fibroblasts in response to the binding of various pro-inflammatory cytokines.
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Synonyms
IRAP, IL1F3, IL1RA; IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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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. Please avoid 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 :
Collagen-I GoatDescription:
Goat Collagen-I
Product # :
PRO-2682Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.
Source
Goat tissues.
Formulation
Collagen-I was lyophilized without additives.
Purity
Greater than 90.0% as determined by SDS-PAGE 90.0%.
More Info
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Introduction
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Collagen-I although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-I should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A6 HumanDescription:
S100 Calcium Binding Protein A6 Human Recombinant
Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.
Product # :
PRO-148Price :
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Description
S100A6 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.
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Synonyms
Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.
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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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.
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 :
S100A7 HumanDescription:
S100 Calcium Binding Protein A7 Human Recombinant
S100 calcium-binding protein A7 (psoriasin 1), S100A7c, PSOR1.
Product # :
PRO-149Price :
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Description
S100A7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.6 kDa.The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A7 protein at 0.5mg/ml in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 30% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A7 is a member of the S-100 family of calcium binding proteins and is produced through a non-classical secretory pathway to the cytoplasm. S100A7 takes part in the regulation of several cellular courses, such as cell cycle, cell progression and cellular differentiation. S100A7 holds two EF-hand domains and is extremely upregulated in psoriatic epidermis, in addition to bladder squamous cell carcinoma and breast cancer tissue, signifying a probable part in carcinogenesis.
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Synonyms
S100 calcium-binding protein A7 (psoriasin 1), S100A7c, PSOR1.
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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 MSNTQAERSI IGMIDMFHKY TRRDDKIDKP SLLTMMKENFPNFLSACDKK GTNYLADVFE KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS Q.
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 :
MIP 1a HumanDescription:
Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
Product # :
CHM-233Price :
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Shipped at Room temp
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Description
Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 0.55 mg/ml solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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 Macrophage Inflammatory Protein-1a 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, Ala-Ser-Leu-Ala-Ala.
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Background
What is the molecular weight/Mw of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein has a total Mw of 7.82kDa.
What is the source or expression system of MIP 1A HUMAN Protein?
Escherichia Coli.
What is the Purity of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A HUMAN Protein?
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of MIP 1A HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.
What applications can MIP 1A HUMAN Protein be used in?
MIP 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A HUMAN Protein?
The endotoxin level is minimal, MIP 1A HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin A E.ColiDescription:
Cyclophilin A E.Coli Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, CypA, rot, rotA.
Product # :
ENZ-859Price :
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Description
Cyclophilin A E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (25-190a.a.) and having a molecular mass of 20.5kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, CypA, rot, rotA.
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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 MGSAKGDPHV LLTTSAGNIE LELDKQKAPV SVQNFVDYVN SGFYNNTTFH RVIPGFMIQG GGFTEQMQQK KPNPPIKNEA DNGLRNTRGT IAMARTADKD SATSQFFINV ADNAFLDHGQ RDFGYAVFGK VVKGMDVADK ISQVPTHDVG PYQNVPSKPV VILSAKVLP.
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 :
DBI HumanDescription:
DBI Human Recombinant
ACBP, ACBD1, CCK-RP, EP, DBI, EP, MGC70414, Acyl-CoA-binding protein, GABA receptor modulator.
Product # :
PRO-832Price :
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Description
DBI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 107 amino acids (1-87a.a.) and having a molecular mass of 12.2kDa. DBI protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
DBI Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DBI, also known as Acyl-CoA-binding protein isoform 2, is a binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.
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Synonyms
ACBP, ACBD1, CCK-RP, EP, DBI, EP, MGC70414, Acyl-CoA-binding protein, GABA receptor modulator.
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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 MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN ELKGTSKEDA MKAYINKVEE LKKKYGI.
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 :
AKT1 HumanDescription:
Protein Kinase B Alpha Human Recombinant
V-Akt Murine Thymoma Viral Oncogene Homolog 1, Protein Kinase B Alpha, Proto-Oncogene C-Akt, RAC-PK-Alpha, EC 2.7.11.1, PKB Alpha, CWS6, PKB, RAC, RAC-Alpha Serine/Threonine-Protein Kinase, Rac Protein Kinase Alpha, Protein Kinase B, PKB-ALPHA, RAC-ALPHA, EC 2.7.11, AKT1m, PRKBA, AKT, RAC-alpha serine/threonine-protein kinase.
Product # :
PKA-068Price :
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Description
AKT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-480 a.a) and having a molecular mass of 58.1kDa. AKT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AKT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Akt1, also known as Akt or else protein kinase B (PKB) is an important molecule in mammaliancellular signaling. In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. Moreover, these enzymes are members of the serine/threonine-specific protein kinase family (EC2.7.11.1). Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesis pathways, and is therefore a key signaling protein in the cellular pathways which lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a most important factor in numerous types of cancer. Akt (now also called Akt1) was at first identified as the oncogenein the transforming retrovirus, AKT8.
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Synonyms
V-Akt Murine Thymoma Viral Oncogene Homolog 1, Protein Kinase B Alpha, Proto-Oncogene C-Akt, RAC-PK-Alpha, EC 2.7.11.1, PKB Alpha, CWS6, PKB, RAC, RAC-Alpha Serine/Threonine-Protein Kinase, Rac Protein Kinase Alpha, Protein Kinase B, PKB-ALPHA, RAC-ALPHA, EC 2.7.11, AKT1m, PRKBA, AKT, RAC-alpha serine/threonine-protein kinase.
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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 MGSMSDVAIV KEGWLHKRGE YIKTWRPRYF LLKNDGTFIG YKERPQDVDQ REAPLNNFSV AQCQLMKTER PRPNTFIIRC LQWTTVIERT FHVETPEERE EWTTAIQTVA DGLKKQEEEE MDFRSGSPSD NSGAEEMEVS LAKPKHRVTM NEFEYLKLLG KGTFGKVILV KEKATGRYYA MKILKKEVIV AKDEVAHTLT ENRVLQNSRH PFLTALKYSF QTHDRLCFVM EYANGGELFF HLSRERVFSE DRARFYGAEI VSALDYLHSE KNVVYRDLKL ENLMLDKDGH IKITDFGLCK EGIKDGATMK TFCGTPEYLA PEVLEDNDYG RAVDWWGLGV VMYEMMCGRL PFYNQDHEKL FELILMEEIR FPRTLGPEAK SLLSGLLKKD PKQRLGGGSE DAKEIMQHRF FAGIVWQHVY EKKLSPPFKP QVTSETDTRY FDEEFTAQMI TITPPDQDDS MECVDSERRP HFPQFSYSAS GTA.
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 :
MYL12A HumanDescription:
Myosin Light Chain 12A Human Recombinant
Myosin regulatory light chain 12A, MLC-2B, Myosin RLC, Myosin regulatory light chain 2 nonsarcomeric, Myosin regulatory light chain MRLC3, MYL12A, MLCB, MRLC3, RLC, MRCL3, MYL2B.
Product # :
PRO-902Price :
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Shipped with Ice Packs
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Description
MYL12A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-171 a.a.) and having a molecular mass of 22.4kDa.MYL12A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYL12A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myosin regulatory light chain 12A (MYL12A) has a vital role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. The MYL12A protein is involved in cytokinesis, receptor capping, and cell locomotion.
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Synonyms
Myosin regulatory light chain 12A, MLC-2B, Myosin RLC, Myosin regulatory light chain 2 nonsarcomeric, Myosin regulatory light chain MRLC3, MYL12A, MLCB, MRLC3, RLC, MRCL3, MYL2B.
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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 MGSHMSSKRT KTKTKKRPQR ATSNVFAMFD QSQIQEFKEA FNMIDQNRDG FIDKEDLHDM LASLGKNPTD EYLDAMMNEA PGPINFTMFL TMFGEKLNGT DPEDVIRNAF ACFDEEATGT IQEDYLRELL TTMGDRFTDE EVDELYREAP IDKKGNFNYI EFTRILKHGA KDKDD.
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 :
Noggin MouseDescription:
Noggin Mouse Recombinant
Noggin, SYM1, SYNS1, NOG.
Product # :
CYT-600Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa (each chain 23.2 kDa).
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% acetonitrile, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg in the presence of 5ng/ml BMP-4.More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
Noggin, SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
CGWIPIQYPIISECKCSC.
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 :
BLyS Human, HisDescription:
B cell Activating Factor Human Recombinant, His Tag
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-545Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 21kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The biological functionality of BLYS Protein will be determined in the future.
What is the amino acid sequence of BLYS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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 :
BMP 7 Human, HisDescription:
Bone Morphogenetic Protein-7 Human Recombinant, His Tag
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Product # :
CYT-629Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
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Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.
What is the source or expression system of BMP7 Protein?
Escherichia Coli.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.
What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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.