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594 results found for “Homeobox”
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Name :
SPP1 Human, HEKDescription:
Osteopontin Human Recombinant, HEK
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
Product # :
CYT-047Price :
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Shipping Method :
Shipped at Room temp
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Description
Osteopontin Human Recombinant is a single, glycosylated, polypeptide chain produced in HEK293 cells, is a full length protein (amino acids 17-314) fused with a polyhistidine tag at the C-terminus, having a total calculated molecular mass of 34.5kDa (The actual molecular mass may be approximately 60-65kDa in SDS-PAGE under reducing conditions due to glycosylation).Osteopontin is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
Osteopontin was lyophilized from a 0.2µM filtered solution of 20mM PBS and 150mM NaCl, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases. -
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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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Solubility
It is recommended to reconstitute the lyophilized SPP1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
IPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETL
PSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDEL
VTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDIT
SHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRK
ANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDS
ASSEVNVDHHHHHH.
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 :
sRANKL (158-316) MouseDescription:
Soluble RANK Ligand (158-316 a.a) Mouse Recombinant
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.
Product # :
CYT-958Price :
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Description
sRANKL Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (158-316 a.a.) and having a molecular mass of 17.9kDa. sRANKL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
sRANKL protein solution (1mg/ml) containing Tris-Hcl buffer pH-8.5 and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells, is less than 2ng/ml.Citations
More Info
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Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
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Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.
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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
MKPEAQPFAH LTINAASIPS GSHKVTLSSW YHDRGWAKIS NMTLSNGKLR VNQDGFYYLY ANICFRHHET SGSVPTDYLQ LMVYVVKTSI KIPSSHNLMK GGSTKNWSGN SEFHFYSINV GGFFKLRAGE EISIQVSNPS LLDPDQDATY FGAFKVQDID
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 :
SYT11 HumanDescription:
Synaptotagmin XI Human Recombinant
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
Product # :
PRO-2301Price :
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Description
SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.
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Synonyms
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-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 MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.
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 :
BD 3 HumanDescription:
Beta Defensin-3 Human Recombinant
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Product # :
CYT-461Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Beta Defensin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 45 amino acids and having a molecular mass of 5161.2 Dalton. The BD-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HBD-3 was lyophilized without additives.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
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Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-3 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
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
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Background
Beta Defensin-3 Human Recombinant: Advancements in Antimicrobial Peptide Therapy
Abstract:
Beta Defensin-3 (hBD-3) human recombinant is a promising antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi. This research paper provides an overview of hBD-3, including its properties, mode of action, and potential applications. Additionally, novel methodologies for the production and optimization of hBD-3 human recombinant are discussed, highlighting its future implications in the field of infectious disease management.Introduction:
The rise of drug-resistant pathogens necessitates exploring alternative therapeutic approaches, such as antimicrobial peptides. Beta Defensin-3 (hBD-3) human recombinant has emerged as a potent candidate due to its broad-spectrum antimicrobial activity. This paper aims to examine the unique features of hBD-3 and propose innovative methodologies for its production and optimization.Properties and Mode of Action:
hBD-3 possesses a distinct structural composition consisting of 45 amino acids, including an N-terminal loop, three antiparallel β-strands, and a C-terminal α-helix. These structural elements contribute to its ability to disrupt microbial membranes and target selectivity. The mode of action involves electrostatic interactions with negatively charged microbial membranes, leading to membrane disruption and subsequent cell death. Furthermore, hBD-3 exhibits immunomodulatory functions by promoting chemotaxis, enhancing phagocytic activity, and modulating the release of pro-inflammatory cytokines.Production of hBD-3 Human Recombinant:
Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored for the efficient production of hBD-3 human recombinant. Each system offers distinct advantages and challenges, requiring careful selection to achieve high yields and desired protein quality. Optimization strategies, including codon optimization, fusion protein tags, and appropriate growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-3 recombinant.Applications and Future Perspectives:
hBD-3 human recombinant exhibits significant therapeutic potential against drug-resistant pathogens, making it a promising alternative to conventional antibiotics. It also demonstrates promise in wound healing and tissue regeneration by stimulating angiogenesis, extracellular matrix production, and keratinocyte migration. Moreover, the unique physicochemical properties of hBD-3 open avenues for its utilization in nanomedicine, enabling targeted therapy and improved drug delivery.Conclusion:
hBD-3 human recombinant represents a potent antimicrobial peptide with broad-spectrum activity against diverse pathogens. The optimization of production methodologies and further exploration of its mechanisms of action will contribute to its clinical utility. With its potential applications in infectious disease management, wound healing, and nanomedicine, hBD-3 human recombinant holds promise as a versatile therapeutic agent.What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 5.1kDa.
What is the source or expression system of BD3 Protein?
Escherichia Coli.
What is the Purity of BD3 Protein?
BD3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BD3 Protein?
The biological functionality of BD3 Protein will be determined in the future.
What is the amino acid sequence of BD3 Protein?
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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 :
BAFF AntibodyDescription:
B-cell Activating Factor, Mouse Anti Human
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B.
Product # :
ANT-367Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
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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.
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Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human BAFF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human BAFF amino acids 134-285 purified from E. coli.
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Ig Subclass
Mouse IgG3 heavy chain and κ light chain.
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Clone
PH4C7AT.
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Applications
BAFF antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.
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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
BAFF antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BID AntibodyDescription:
BH3 Interacting Domain Death Agonist , Mouse Anti Human
BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355.
Product # :
ANT-353Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
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Introduction
BID accession number NP_001187 is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which leads to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.
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Synonyms
BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355.
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Immunogen
Anti-human BID mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human BID amino acids 1-195 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P4D3AT.
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Applications
BID antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000.Recommended starting dilution is 1:1,000.
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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
BID antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Acrp30 AntibodyDescription:
Adiponectin, Mouse Anti Human
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
ANT-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
containing PBS, pH-7.4, & 0.1% Sodium Azide
Citations
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Introduction
Human Adiponectin is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. APM-1 plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Sterile Filtered solution.
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Immunogen
Anti-human adiponectin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human adiponectin amino acids 15-244 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
P1G12AT.
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Applications
Adiponectin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:250 ~ 1:1,000. The antibody has the specificity against globular domain of adiponectin. Recommended starting dilution is 1:500.
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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
Adiponectin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NQO2 AntibodyDescription:
NAD(P)H Dehydrogenase Quinone 2, Mouse Anti Human
DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].
Product # :
ANT-024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
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Introduction
NQO2 is a flavoprotein that catalyzes the 2-electron reduction of diverse quinones, redox dyes, and the vitamin K menadione. NQO2 mainly uses dihydronicotinamide riboside (NRH) as the electron donor. NQO2 catalyzes the metabolic detoxification of quinones and their derivatives to hydroquinones. This detoxification process protects cells against quinone-induced oxidative stress, cytotoxicity and mutagenicity.
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Synonyms
DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human NQO2 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NQO2 amino acids 1-231 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PAT1E3AT.
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Applications
NQO2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:250 ~ 500.
Recommended starting dilution is 1:500. -
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
NQO2 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HA Monoclonal AntibodyDescription:
HA Mouse Antibody
Product # :
ANT-225Price :
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Description
Monoclonal antibodies are produced by immunizing mouse with synthetic peptide (YPYDVPDYA) coupled to KLH.
Formulation
1×PBS & 50% glycerol.
Citations
More Info
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Physical Appearance
Sterile filtered colorless solution.
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Ig Subclass
Mouse IgG1.
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Clone
PHASHG.
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Applications
Western Blot, Immunoprecipitation.
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Titer
Western Blotting: 1µg/ml.
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Type
Mouse Antibody 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.
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 :
ANXA1 AntibodyDescription:
Annexin A1, Mouse Anti Human
ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.
Product # :
ANT-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
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Introduction
ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.
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Synonyms
ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human ANXA1 mAb, clone PAT2G5AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ANXA1 protein 1-346 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT2G5AT
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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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
ANXA1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EIF4E MouseDescription:
Eukaryotic Translation Initiation Factor 4E Recombinant Mouse
eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.
Product # :
PRO-2411Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EIF4E Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (1-217 a.a) and having a molecular mass of 27.6kDa. EIF4E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EIF4E protein solution (1mg/ml) 20mM Tris-HCl Buffer (pH8.0), 10% glycerol, 1mM DTT, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.
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Synonyms
eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.
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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 MGSHMATVEP ETTPTTNPPP AEEEKTESNQ EVANPEHYIK HPLQNRWALW FFKNDKSKTW QANLRLISKF DTVEDFWALY NHIQLSSNLM PGCDYSLFKD GIEPMWEDEK NKRGGRWLIT LNKQQRRSDL DRFWLETLLC LIGESFDDYS DDVCGAVVNV RAKGDKIAIW TTECENRDAV THIGRVYKER LGLPPKIVIG YQSHADTATK SGSTTKNRFV V
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 :
SEMAXDescription:
SEMAX
Product # :
HOR-033Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- formulation
- purity
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Description
SEMAX Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 813.92 Dalton and a Molecular formula of C37H51N19O1S.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SEMAX although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SEMAX 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 SEMAX 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-Met-Glu-His-Phe-Pro-Gly-Pro-OH.
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Background
Semax, also known as ACTH(4-10) Pro-Gly-Pro, is a synthetic peptide that has been the subject of extensive research due to its potential neuroprotective and nootropic effects. This heptapeptide, derived from the adrenocorticotropic hormone (ACTH), has been shown to possess a wide range of biological activities, including enhancing memory, learning, and neurogenesis.
Semax is unique in its ability to cross the blood-brain barrier and exert its effects directly on the central nervous system. It has been shown to stimulate the release of brain-derived neurotrophic factor (BDNF), a protein that plays a crucial role in the survival of neurons and the growth of new neurons and synapses. Studies by Dolotov et al. (2006) have demonstrated that Semax can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its nootropic effects, Semax has been shown to possess neuroprotective properties. Research by Stavchansky et al. (2008) found that Semax could protect neurons from oxidative stress and apoptosis, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its nootropic and neuroprotective effects, Semax has been proposed as a potential therapeutic agent for a variety of conditions, including cognitive disorders, stroke, and optic nerve disease. For instance, a study by Myasoedov et al. (2010) found that Semax could improve outcomes in patients with ischemic stroke, indicating its potential as a therapeutic agent in stroke recovery.
While research on Semax 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 Semax in humans. However, the existing body of research suggests that Semax could be a promising tool in the treatment of cognitive disorders and neurodegenerative diseases.
What is the molecular weight/Mw of SEMAX Protein?
SEMAX Protein has a total Mw of 0.813kDa.
What is the Purity of SEMAX Protein?
SEMAX Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of SEMAX Protein?
The biological functionality of SEMAX Protein will be determined in the future.
What is the amino acid sequence of SEMAX Protein?
H-Met-Glu-His-Phe-Pro-Gly-Pro-OH.
What applications can SEMAX Protein be used in?
SEMAX Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for SEMAX Protein?
The endotoxin level is minimal, SEMAX Protein was purified using conventional chromatography techniques.
Who supplies SEMAX that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of SEMAX?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
MMP2 HumanDescription:
Matrix Metalloproteinase-2 Human Recombinant
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Product # :
ENZ-769Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
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- purity
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Description
MMP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 576 amino acids (110-660a.a) and having a molecular mass of 64.7kDa. MMP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).
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Synonyms
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
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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 MGSEFYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARAFQVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGKEY NSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NAEGQPCKFP FRFQGTSYDS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRSDGKMW CATTANYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS QDDIKGIQEL YGASPDIDLG TGPTPTLGPV TPEICKQDIV FDGIAQIRGE IFFFKDRFIW RTVTPRDKPM GPLLVATFWP ELPEKIDAVY EAPQEEKAVF FAGNEYWIYS ASTLERGYPK PLTSLGLPPD VQRVDAAFNW SKNKKTYIFA GDKFWRYNEV KKKMDPGFPK LIADAWNAIP DNLDAVVDLQ GGGHSYFFKG AYYLKLENQS LKSVKFGSIK SDWLGC.
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 :
Myostatin HumanDescription:
Myostatin Human Recombinant
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-418Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- biological activity
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Description
Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.Citations
More Info
-
Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin 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 Myostatin in sterile 20mM HCl at 0.1 mg/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-Phe-Gly-Leu-Asp.
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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 1.55 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 Myostatin 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.
- View Data Sheet
Name :
SelankDescription:
SELANK
Product # :
HOR-035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SELANK Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 751.89 Dalton and a Molecular formula of C33H57N11O9.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SELANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELANK 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 SELANK 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-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.
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Background
Selank, also known as TP-7, is a synthetic peptide that has garnered significant attention in the scientific community due to its potential anxiolytic, neuroprotective, and nootropic effects. This heptapeptide, derived from the naturally occurring human tetrapeptide Tuftsin, has been shown to possess a wide range of biological activities, including enhancing memory, reducing anxiety, and potentially mitigating the effects of neurodegenerative diseases.
Selank's primary mechanism of action involves its interaction with the GABAergic system, the body's main inhibitory neurotransmitter system. By modulating the activity of GABA receptors, Selank can exert a calming effect on the brain, reducing anxiety and enhancing cognitive function. Studies by Semenova et al. (2014) have demonstrated that Selank can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its anxiolytic and nootropic effects, Selank has been shown to possess neuroprotective properties. Research by Ershov et al. (2016) found that Selank 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 anxiolytic, nootropic, and neuroprotective effects, Selank has been proposed as a potential therapeutic agent for a variety of conditions, including anxiety disorders, cognitive disorders, and neurodegenerative diseases. For instance, a study by Medvedev et al. (2017) found that Selank could improve symptoms in patients with generalized anxiety disorder, indicating its potential as a therapeutic agent in the treatment of anxiety disorders.
While research on Selank 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 Selank in humans. However, the existing body of research suggests that Selank could be a promising tool in the treatment of anxiety disorders, cognitive disorders, and neurodegenerative diseases.
What is the molecular weight/Mw of SELANK Protein?
SELANK Protein has a total Mw of 0.751kDa.
What is the Purity of SELANK Protein?
SELANK Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of SELANK Protein?
The biological functionality of SELANK Protein will be determined in the future.
What is the amino acid sequence of SELANK Protein?
H-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.
What applications can SELANK Protein be used in?
SELANK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for SELANK Protein?
The endotoxin level is minimal, SELANK Protein was purified using conventional chromatography techniques.
Who supplies SELANK that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of SELANK?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
IL 24 HumanDescription:
Interleukin-24 Human Recombinant
C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.
Product # :
CYT-515Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin 24 human recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18 kDa. As a result of glycosylation, the protein migrates at 19.5 kDa on SDS-PAGE.
Source
Sacharomyces cerevisiae.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS with BSA as a carrier.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind to the cell receptor of Capan-1 cells line resulted in Stat-3 activation. The ED50 for this effect is typically 1.0 ng/ml, corresponding to a Specific Activity of 1x106 units/mg.Citations
More Info
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Introduction
IL24 is a member of the IL10 family of cytokines. It was identified as a gene induced during terminal differentiation in melanoma cells. IL-10B encoded can induce apoptosis selectively in various cancer cells. Overexpression IL-24 leads to elevated expression of several GADD family genes, which correlates with the induction of apoptosis. The phosphorylation of mitogen-activated protein kinase 14 (MAPK7/P38), and heat shock 27kDa protein 1 (HSPB2/HSP27) are found to be induced by this gene in melanoma cells, but not in normal immortal melanocytes. Alternatively spliced transcript variants encoding distinct isoforms have been reported. The glycosylation is essential for activity of IL-24. Functionally, IL-24 has diverse activities. At low concentrations, it induces type I proinflammatory cytokines such as IFN-g, IL-1b, IL-12 and TNF-a. At high concentration, it is a strong inducer of apoptosis in tumor cells, but not normal cells. mda-7/IL-24 is being hailed as a ‘magic bullet’ for cancer gene therapy.
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Synonyms
C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MDA7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MDA-7 Recombinant 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 IL-24 in sterile 18MΩ-cm H2O 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.
- View Data Sheet
Name :
FGF23 HumanDescription:
Fibroblast Growth Factor-23 Human Recombinant
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Product # :
CYT-020Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- purity
- biological activity
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Description
Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
Citations
More Info
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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
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Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
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Background
Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.
Mechanism
Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.Interactions
Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.Function
Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.Structure
FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.What is the molecular weight/Mw of FGF23 HUMAN Protein?
FGF23 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of FGF23 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF23 HUMAN Protein?
FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF23 HUMAN Protein?
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
What is the amino acid sequence of FGF23 HUMAN Protein?
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
What applications can FGF23 HUMAN Protein be used in?
FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF23 HUMAN Protein?
The endotoxin level is minimal, FGF23 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.
- View Data Sheet
Name :
VEGF (121 a.a.) HumanDescription:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-343Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.
Citations
More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor -121 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
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R
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.