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1000 results found for “Periostin”
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Name :
PSMB8 HumanDescription:
Proteasome Subunit Beta Type 8 Human Recombinant
D6S216, D6S216E, LMP7, MGC1491, PSMB5i , Low molecular mass protein 7 Macropain subunit C13, Multicatalytic endopeptidase complex subunit C13,Proteasome component C13, Proteasome subunit beta-5i, Really interesting new gene 10 protein.
Product # :
ENZ-670Price :
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Shipped with Ice Packs
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Description
PSMB8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (73-276 a.a.) and having a molecular mass of 25.4kDa. PSMB8 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PSMB8 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
Proteasome Subunit Beta Type 8 (PSMB8) is a member of the peptidase T1B family. The proteasome is a multicatalytic proteinase complex with well-organized ring-shaped 20S core structure. Proteasomes are spread through eukaryotic cells at a high concentration. PSMB8 is mainly expressed in immature dendritic cells. vital function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.PSMB8 is positioned in the class II region of the MHC (main histocompatibility complex). PSMB8 plays as a significant factor of INFG-induced sensitivity and in apoptosis by degradation of the apoptotic inhibitor MCL1.
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Synonyms
D6S216, D6S216E, LMP7, MGC1491, PSMB5i , Low molecular mass protein 7 Macropain subunit C13, Multicatalytic endopeptidase complex subunit C13,Proteasome component C13, Proteasome subunit beta-5i, Really interesting new gene 10 protein.
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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 MGSHMTTTLA FKFQHGVIAA VDSRASAGSY ISALRVNKVI EINPYLLGTM SGCAADCQYW ERLLAKECRL YYLRNGERIS VSAASKLLSN MMCQYRGMGL SMGSMICGWD KKGPGLYYVD EHGTRLSGNM FSTGSGNTYA YGVMDSGYRP NLSPEEAYDL GRRAIAYATH RDSYSGGVVN MYHMKEDGWV KVESTDVSDL LHQYREANQ.
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 :
PVALB HumanDescription:
Parvalbumin Human Recombinant
Parvalbumin alpha, PVALB, D22S749, MGC116759.
Product # :
PRO-004Price :
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Description
PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.
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Synonyms
Parvalbumin alpha, PVALB, D22S749, MGC116759.
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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 MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.
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 :
COQ9 HumanDescription:
Coenzyme Q9 Human Recombinant
Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.
Product # :
ENZ-898Price :
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Description
COQ9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (45-318 a.a) and having a molecular mass of 33.3kDa.COQ9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COQ9 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquinone biosynthesis protein COQ9 (COQ9) represents a mitochondrial ubiquinone biosynthesis gene. The COQ9 protein is likely required for biosynthesis of coenzyme Q10, since mutations at this locus have been linked with autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency.
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Synonyms
Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.
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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 MGSRSSDEQK QQPPNSFSQQ HSETQGAEKP DPESSHSPPR YTDQGGEEEE DYESEEQLQH RILTAALEFV PAHGWTAEAI AEGAQSLGLS SAAASMFGKD GSELILHFVT QCNTRLTRVL EEEQKLVQLG QAEKRKTDQF LRDAVETRLR MLIPYIEHWP RALSILMLPH NIPSSLSLLT SMVDDMWHYA GDQSTDFNWY TRRAMLAAIY NTTELVMMQD SSPDFEDTWR FLENRVNDAM NMGHTAKQVK STGEALVQGL MGAAVTLKNL TGLNQRR.
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 :
RCN1 HumanDescription:
Reticulocalbin 1 Human Recombinant
PIG20, RCAL, RCN.
Product # :
PRO-544Price :
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Description
RCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (30-331 a.a.) and having a molecular mass of 40.4kDa (real molecular weight on SDS-PAGE will be shift up). The RCN1 is fused to 39 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
RCN1 is a calcium-binding protein which binds calcium and controls calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. RCN1 withholds six conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.
High conservation of amino acid residues outside of these motifs, in relation to mouse reticulocalbin, is consistent with a biochemical function further to that of calcium binding. In human endothelial and prostate cancer cell lines RCN1 protein is localized to the plasma membrane. -
Synonyms
PIG20, RCAL, RCN.
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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 KDRWGSELEK PTVRKERVVR PDSELGERPP EDNQSFQYDH EAFLGKEDSK TFDQLTPDES
KERLGKIVDR IDNDGDGFVT TEELKTWIKR VQKRYIFDNV AKVWKDYDRD KDDKISWEEY KQATYGYYLG NPAEFHDSSD HHTFKKMLPR
DERRFKAADL NGDLTATREE FTAFLHPEEF EHMKEIVVLE TLEDIDKNGD GFVDQDEYIA DMFSHEENGP EPDWVLSERE QFNEFRDLNK
DGKLDKDEIR HWILPQDYDH AQAEARHLVY ESDKNKDEKL TKEEILENWN MFVGSQATNY GEDLTKNHDE L.
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 :
RELM g MouseDescription:
RELM-Gamma Mouse Recombinant
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-1035Price :
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Shipped at Room temp
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Description
RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
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Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.
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 :
REXO1 HumanDescription:
RNA Exonuclease 1 Human Recombinant
RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.
Product # :
ENZ-767Price :
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Description
REXO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1060-1221a.a) and having a molecular mass of 22.3kDa. REXO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The REXO1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
REXO1 is an exonuclease domain-containing protein which binds to Elongin. The Elongin complex stimulates the rate of transcription elongation by RNA polymerase II by suppressing the transient pausing of the polymerase at many sites along the DNA template. REXO1 is composed of 1221 amino acids and its mRNA is ubiquitously expressed. REXO1 is a putative stem cell marker and is highly expressed in embryonic and adult stem cells.
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Synonyms
RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.
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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 KDRWGSIYAL DCEMSYTTYG LELTRVTVVD TDVHVVYDTF VKPDNEIVDY NTRFSGVTEA DLADTSVTLR DVQAVLLSMF SADTILIGHS LESDLLALKV IHSTVVDTSV LFPHRLGLPY KRSLRNLMAD YLRQIIQDNV DGHSSSEDAG ACMHLVIWKV REDAKTKR.
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 :
RGS10 HumanDescription:
Regulator of G-Protein Signaling 10 Human Recombinant
Regulator Of G-Protein Signaling 10, RGS10.
Product # :
PRO-890Price :
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Description
RGS10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-181) and having a molecular mass of 23.7 kDa.The RGS10 is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RGS10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
RGS10 is a member of the RGS family that regulate molecules which perform as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins can disengage G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. The nucleus localized RGS10 is associates specifically with the activated forms of the two related G-protein subunits, G-alphai3 and G-alphaz but is unable to cooperate with the structurally and functionally distinct G-alpha subunits.
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Synonyms
Regulator Of G-Protein Signaling 10, RGS10.
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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 MGSHMFNRAV SRLSRKRPPS DIHDSDGSSS SSHQSLKSTA KWAASLENLL EDPEGVKRFR EFLKKEFSEE NVLFWLACED FKKMQDKTQM QEKAKEIYMT FLSSKASSQV NVEGQSRLNE KILEEPHPLM FQKLQDQIFN LMKYDSYSRF LKSDLFLKHK RTEEEEEDLP DAQTAAKRAS RIYNT
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL8 Human (1-72)Description:
Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-231Price :
Quantity :
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Shipped at Room temp
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Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.
What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
What applications can CXCL8 HUMAN (1-72) Protein be used in?
CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-72) Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FIS1 HumanDescription:
Fission-1 Human Recombinant
TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).
Product # :
PRO-829Price :
Quantity :
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Shipped with Ice Packs
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Description
FIS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids (1-122 a.a.) and having a molecular mass of 16.3 kDa. FIS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
FIS1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 induces cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. FIS1 participates in peroxisomal growth and division. The C terminus is required for mitochondrial localisation, while the N teminus is necessary for mitochondrial fission.
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Synonyms
TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).
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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 MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK DG.
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 :
PARP1 HumanDescription:
Poly (ADP-Ribose) Polymerase 1 Human Recombinant
ADPRT, ADPRT1, pADPRT, pADPRT-1, PARP, PARP-1, PPOL, Poly [ADP-ribose] polymerase 1, NAD(+) ADP-ribosyltransferase 1, Poly[ADP-ribose] synthase 1, PARP1.
Product # :
ENZ-477Price :
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Shipped with Ice Packs
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Description
PARP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 354 amino acids (662-1014a.a.) and having a molecular mass of 39.6 kDa. PARP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PARP1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PARP1 takes part in the base excision repair pathway, by catalyzing the poly ADP-ribosyl of a restricted number of acceptor proteins involved in chromatin architecture and in DNA metabolism.. PARP1 mediates the poly ADP-ribosy of APLF and CHFR. PARP1 positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. PARP1 is a chromatin-associated enzyme, poly (ADP-ribosyl) transferase, which modifies various nuclear proteins by poly ADP-ribosyl. PARP1 takes part in the regulation of various significant cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. PARP1 is a site of mutation in Fanconi anemia, and is involved in the pathophysiology of type I diabetes.
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Synonyms
ADPRT, ADPRT1, pADPRT, pADPRT-1, PARP, PARP-1, PPOL, Poly [ADP-ribose] polymerase 1, NAD(+) ADP-ribosyltransferase 1, Poly[ADP-ribose] synthase 1, PARP1.
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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
MKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KAEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW.
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 :
LGALS3 Human, HisDescription:
Galectin-3 Human Recombinant, His Tag
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Product # :
CYT-693Price :
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- sds-page
Description
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 270 amino acids (1-250 a.a.) and having a molecular mass of 28.3 kDa. The LGALS3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is < 15ug/ml as measured by its ability to agglutinate human red blood cells.sds-page
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
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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 MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.
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Background
What is the molecular weight/Mw of LGALS3 HUMAN, HIS Protein?
LGALS3 HUMAN, HIS Protein has a total Mw of 28.3kDa.
What is the source or expression system of LGALS3 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS3 HUMAN, HIS Protein?
LGALS3 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 HUMAN, HIS Protein?
The ED50 for this effect is < 2.5ug/ml as measured by its ability to agglutinate human red blood cells.
What is the amino acid sequence of LGALS3 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.
What applications can LGALS3 HUMAN, HIS Protein be used in?
LGALS3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS3 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Eotaxin Human, HisDescription:
Eotaxin Human Recombinant (CCL11), His Tag
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-344Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Eotaxin His Tag Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids fragment (24-87) corresponding to the mature Eotaxin protein and having a molecular mass of 8345.9 Dalton with an amino-terminal hexahistidine tag.The Eotaxin-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Eotaxin-His is supplied liquid In Phosphate Buffered Saline pH7.4 containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE
More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
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Background
What is the molecular weight/Mw of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein has a total Mw of 8.34kDa.
What is the source or expression system of EOTAXIN HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN, HIS Protein?
The biological functionality of EOTAXIN HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of EOTAXIN HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
What applications can EOTAXIN HUMAN, HIS Protein be used in?
EOTAXIN HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN, HIS Protein?
The endotoxin level is minimal, EOTAXIN HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Visfatin AntibodyDescription:
Visfatin, Mouse Anti Human
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
ANT-368Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.
More Info
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Introduction
Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-α, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It h
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Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Immunogen
Anti-human Visfatin mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Visfatin amino acids 1-491 purified from E. coli.
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Ig Subclass
Mouse IgG1heavy chain and κ light chain.
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Clone
P4D5AT.
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Applications
Visfatin 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.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
Visfatin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OPG Fc HumanDescription:
Osteoprotegerin Human Recombinant /Fc Chimera
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
Product # :
CYT-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant OPG produced in yeast contains 2x412 amino acid residues, including 180 residues from mature OPG (a.a 22-201) and 232 residues from the Fc protein of human IgG1, and has a calculated molecular mass of 109.6kDa.
Source
Pichia Pastoris.
Formulation
OPG was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 6.0, 150mM NaCl and 0.02 % Tween-80.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by neutralizing the stimulation of U937 cells is less tha10ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10ng/ml soluble Human RANKL (sRANKL).
More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin 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
OPG 22-201 ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL
Fc232EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKTISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK
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 :
STAT3 HumanDescription:
Signal Transducer and Activator of Transcription 3 Human Recombinant
Signal transducer and activator of transcription 3 isoform 1, STAT3, ADMIO, DMIO1, APRF, HIES.
Product # :
PKA-113Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STAT3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (1-770 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 776 amino acids and having a molecular mass of 88.8kDa.STAT3 shows multiple bands between 70-100kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
STAT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol& 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Signal transducer and activator of transcription 3 isoform 1, STAT3, ADMIO, DMIO1, APRF, HIES.
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Synonyms
Signal transducer and activator of transcription 3 isoform 1, STAT3, ADMIO, DMIO1, APRF, HIES.
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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
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL LGEIDQQYSR FLQESNVLYQ HNLRRIKQFLQSRYLEKPME IARIVARCLW EESRLLQTAA TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL ADWKRRQQIA CIGGPPNICL DRLENWITSLAESQLQTRQQ IKKLEELQQK VSYKGDPIVQ HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGLKIDLETHSLP VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST KPPGTFLLRF SESSKEGGVT FTWVEKDISGKTQIQSVEPY TKQQLNNMSF AEIIMGYKIM DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDME LTSECATSPM 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.
- View Data Sheet
Name :
CHGA Human, Sf9Description:
Chromogranin A Human Recombinant, Sf9
CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.
Product # :
PRO-2513Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-457 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 448 amino acids and having a molecular mass of 50kDa.CHGA shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CHGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol & 0.1mM PMSF.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromogranin-A Isoform 1 Preproprotein or CHGA is part of the neuroendocrine secretory proteins of the chromogranin/secretogranin family. CHGA is a precursor of numerus enzymes such as pancreastatin, catestatin, vasostatin-1,vasostatin-2, and parastatin. The protein acts as a negative regulator the neuroendocrine activity of autocrine or nearby cells (paracrine). CHGA causes further production of secretory granules that contains insulin in pancreatic islet beta cells.
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Synonyms
CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLLPVNSPM NKGDTEVMKC IVEVISDTLS KPSPMPVSQE CFETLRGDER ILSILRHQNL LKELQDLALQ GAKERAHQQK KHSGFEDELS EVLENQSSQA ELKEAVEEPS SKDVMEKRED SKEAEKSGEA TDGARPQALP EPMQESKAEG NNQAPGEEEE EEEEATNTHP PASLPSQKYP GPQAEGDSEG LSQGLVDREK GLSAEPGWQA KREEEEEEEE EAEAGEEAVP EEEGPTVVLN PHPSLGYKEI RKGESRSEAL AVDGAGKPGA EEAQDPEGKG EQEHSQQKEE EEEMAVVPQG LFRGGKSGEL EQEEERLSKE WEDSKRWSKM DQLAKELTAE KRLEGQEEEE DNRDSSMKLS FRARAYGFRG PGPQLRRGWR PSSREDSLEA GLPLQVRGYP EEKKEEEGSA NRRPEDQELE SLSAIEAELE KVAHQLQALR RGHHHHHH.
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 :
REN Human, sf9Description:
Renin Human Recombinant, sf9
REN, HNFJ2, Renin, Angiotensinogenase.
Product # :
PRO-2342Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
REN Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (24-406) and having a molecular mass of 43.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).REN is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
REN protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
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Synonyms
REN, HNFJ2, Renin, Angiotensinogenase.
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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
LPTDTTTFKR IFLKRMPSIR ESLKERGVDM ARLGPEWSQP MKRLTLGNTT SSVILTNYMD TQYYGEIGIG TPPQTFKVVF DTGSSNVWVP SSKCSRLYTA CVYHKLFDAS DSSSYKHNGT ELTLRYSTGT VSGFLSQDII TVGGITVTQM FGEVTEMPAL PFMLAEFDGV VGMGFIEQAI GRVTPIFDNI ISQGVLKEDV FSFYYNRDSE NSQSLGGQIV LGGSDPQHYE GNFHYINLIK TGVWQIQMKG VSVGSSTLLC EDGCLALVDT GASYISGSTS SIEKLMEALG AKKRLFDYVV KCNEGPTLPD ISFHLGGKEY TLTSADYVFQ ESYSSKKLCT LAIHAMDIPP PTGPTWALGA TFIRKFYTEF DRRNNRIGFA LARLEHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
STIP1 Human, HisDescription:
Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
Product # :
PRO-753Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.
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Synonyms
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
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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 MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Y.Enterocolitica (O:9) YopBDescription:
Yersinia Enterocolitica (O:9) YopB Recombinant
Protein YopD, pYV0054.
Product # :
PRO-2575Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Yersinia Enterocolitica (O:9) YopB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain having a calculated molecular mass of 43kDa. Y.Enterocolitica (O:9) YopB is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Y.Enterocolitica (O:9) YopB is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Gastroenteritis which has been identified as caused by Yersinia Enterocolitica has been discovered by virulent isolates of the bacteria. During infection, pores are being formed in the presence of adapter protein Yersiniosis. YopB's Interaction with the target membrane to form pores enables the entrance of YopE effectors to the cytoplasmic space of the host’s cell.
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Synonyms
Protein YopD, pYV0054.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Activity
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with positive/negative samples.
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 :
SIGLEC5 HumanDescription:
Sialic Acid Binding Ig Like Lectin 5 Human Recombinant
Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.
Product # :
PRO-2432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIGLEC5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 667 amino acids (17-441a.a.) and having a molecular mass of 74.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC5 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SIGLEC5 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Sialic Acid Binding Ig Like Lectin 5, also known as SIGLEC5 is a member of the immunoglobulin superfamily and SIGLEC family. SIGLEC5 contains of 2 Ig-like C2-type domains and 1 Ig-like V-type domain. In addition, SIGLEC5 is expressed by monocytic/myeloid lineage cells. SIGLEC5 is expressed at high levels in peripheral blood leukocytes, spleen, and at lower levels in lymph node, appendix, pancreas, lung, and thymus.
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Synonyms
Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.
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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
ADLEKPVYEL QVQKSVTVQE GLCVLVPCSF SYPWRSWYSS PPLYVYWFRD GEIPYYAEVV ATNNPDRRVK PETQGRFRLL GDVQKKNCSL SIGDARMEDT GSYFFRVERG RDVKYSYQQN KLNLEVTALI EKPDIHFLEP LESGRPTRLS CSLPGSCEAG PPLTFSWTGN ALSPLDPETT RSSELTLTPR PEDHGTNLTC QMKRQGAQVT TERTVQLNVS YAPQTITIFR NGIALEILQN TSYLPVLEGQ ALRLLCDAPS NPPAHLSWFQ GSPALNATPI SNTGILELRR VRSAEEGGFT CRAQHPLGFL QIFLNLSVYS LPQLLGPSCS WEAEGLHCRC SFRARPAPSL CWRLEEKPLE GNSSQGSFKV NSSSAGPWAN SSLILHGGLS SDLKVSCKAW NIYGSQSGSV LLLQGRSNLG TGVVPAALLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
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 :
GDNF Human, Sf9Description:
Glial-Derived Neurotrophic Factor Human Recombinant, Sf9
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
Product # :
CYT-1162Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GDNF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.
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Synonyms
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
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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
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
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Background
What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.
What is the source or expression system of GDNF HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF HUMAN, SF9 Protein?
The biological functionality of GDNF HUMAN, SF9 Protein will be determined in the future.
What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
What applications can GDNF HUMAN, SF9 Protein be used in?
GDNF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF HUMAN, SF9 Protein?
The endotoxin level is minimal, GDNF HUMAN, SF9 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 :
HCV NS3, BiotinDescription:
Hepatitis C Virus NS3, Biotin Recombinant
Product # :
HCV-244Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
The E.coli derived recombinant Biotin Labeled protein contains the HCV NS3 immunodominant regions, a.a. 1450-1643, 22 kDa. The Biotin labeled protein is fused with a 6xHis-Tag at N-terminus.
Formulation
(1mg/ml) 1.5M urea, 20mM Tris-HCl pH 8.0 and 10mM β-mercaptoethanol.
Purity
HCV NS3 Biotin labeled protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS3 Biotin although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HCV NS3 Biotin labeled antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Reactivity with human HCV positive serum undetermined.
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Purification Method
HCV NS3 Biotin labeled protein was purified by proprietary chromatographic technique.
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 :
Transferrin Human, CHODescription:
Transferrin Human Recombinant, CHO
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2782Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.
Source
Chinese Hamster Ovary cells.
Formulation
Transferrin solution contains 0.05% NaN3 and PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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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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Applications
Immunoassay, cell culture.
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Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.
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 :
DSIPDescription:
Delta Sleep Inducing Peptide
Product # :
HOR-030Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- formulation
- purity
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Description
DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized DSIP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DSIP 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 DSIP in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
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Background
Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.
DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.
In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.
While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative 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.