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1000 results found for “aprotinin”
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Name :
C4c HumanDescription:
Complement Component C4c Human
Complement C4c, Complement Component C4c, C4c.
Product # :
PRO-556Price :
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Shipped with Ice Packs
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Description
Human C4c produced in Human plasma having a molecular mass of 210 kDa.
Source
Human Plasma.
Formulation
The Human Complement C4c solution is in Sodium Phosphate buffer pH 7.0 containing 0.15M NaCl and 0.09% NaN3.
Purity
Greater than 99.0%.
More Info
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Introduction
Complement C4c is a degradation product of C4b which is cleaved by C4b/C3b inactivator to yield C4d and C4c.
Complement C4c interacts with C1 and C2 to form C3 convertase of the classic activation pathway. Systemic lupus erythematosus (SLE) is often associated with congenital C4 deficiency. Reduced levels of components of the classic pathway (C1, C2, C4, C3) are common after such activation, e.g. in SLE, acute serum sickness and conditions associated with circulating immune complexes. -
Synonyms
Complement C4c, Complement Component C4c, C4c.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Human C4c although stable at 4°C for 1 week, should be stored at -15°C.Please avoid freeze-thaw cycles.
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Human Virus Test
Plasma from each donor has been tested and found negative for HIV-1 & 2 antibodies, Hepatatis B surface antigen, and Hepatatis C antibodies.
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 :
LBP HumanDescription:
Lipopolysaccaride Human Recombinant
Lipopolysaccharide-binding protein, LBP, MGC22233.
Product # :
PRO-538Price :
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Shipped at Room temp
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Description
The Lipopolysaccharide Binding Protein is produced from human LBP transfected CHO-cells in serum free medium. Before transfection the complete human LBP-cDNA was amplified by PCR and cloned into expression vector p-POL-DHFR.The recombinant Human LBP was purified by his-tag with metal affinity purification with Talon and controlled by SDS page. Showing a 58kDa band on SDS-PAGE.Attention: His-tag has no protease site and can not be split off.
Source
Chinese Hamster Ovarian Cells (CHO).
Formulation
Recombinant Human LBP was lyophilized from a protein solution (0.3mg/ml) containing phosphate-buffered saline, pH 7.2.
Biological Activity
Up to 0.2 µg/ ml LBP mediates binding of FITC-LPS (0.5µg/ml) to CD14+CHO transfectants (FACS).
More Info
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Introduction
Lipopolysaccharides (LPS) are a type of glycolipids on the outer cell wall of Gram-negative bacteria. Lipopolysaccharide binding protein (aka LBP) is a plasma protein which facilitates the diffusion of bacterial LPS (endotoxin). LBP is involved in the acute-phase immunologic response to gram-negative bacterial infections. In cooperation with bactericidal permeability-increasing protein (BPI), LBP binds LPS and interacts with the CD14 receptor, most likely playing a role in regulating LPS-dependent monocyte responses. LBP belongs to a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). The LBP gene is found on chromosome 20, directly downstream of the BPI gene. LBP catalyzes the transfer of LPS monomers from LPS aggregates to HDL particles, to phospholipid bilayers, and to a binding site on soluble CD14 (sCD14). sCD14 is capable of speeding up the transfer by receiving an LPS monomer from an LPS aggregate, and then yielding it to an HDL particle, therefore acting as a soluble "shuttle" for an insoluble lipid.
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Synonyms
Lipopolysaccharide-binding protein, LBP, MGC22233.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LBP Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LBP 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
Every 10µg of recombinant human LBP should be reconstituted using 33µl of sterile H2O. The solution can be than diluted with phosphate-buffered saline or other buffers.
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 :
DEFB116 HumanDescription:
Beta Defensin 116 Human Recombinant
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Product # :
CYT-713Price :
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Shipped with Ice Packs
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Description
DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
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Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
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Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:
Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.Introduction:
Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.Antimicrobial Properties:
BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.Therapeutic Implications:
The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.Conclusion:
Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.
What is the source or expression system of DEFB116 Protein?
Escherichia Coli.
What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.
What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 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 :
SERF2 HumanDescription:
Small EDRK-Rich Factor 2 Human Recombinant
Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.
Product # :
PRO-1730Price :
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Shipped with Ice Packs
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Description
SERF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (1-59 a.a) and having a molecular mass of 9.3kDa.SERF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SERF2 (small EDRK-rich factor 2) is a member of the SERF family. SERF2 is a protein-coding gene. Among the diseases associated with SERF2 are spinal muscular atrophy, and muscular atrophy.
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Synonyms
Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.
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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 MGSMTRGNQR ELARQKNMKK QSDSVKGKRR DDGLSAAARK QRDSEIMQQK QKKANEKKEE PK
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 :
CXCL1 Mouse, HisDescription:
GRO/KC (CXCL1) Mouse Recombinant, His Tag
Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.
Product # :
CHM-002Price :
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Shipped with Ice Packs
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Description
GRO1/KC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (25-96 a.a.) and having a molecular mass of 10.5kDa.GRO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GRO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.
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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 MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.
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Background
What is the molecular weight/Mw of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein has a total Mw of 10.5kDa.
What is the source or expression system of CXCL1 MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 MOUSE, HIS Protein?
The biological functionality of CXCL1 MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL1 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.
What applications can CXCL1 MOUSE, HIS Protein be used in?
CXCL1 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL1 MOUSE, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Thymosin β4Description:
Thymosin-b4 Human Recombinant
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
Product # :
HOR-003Price :
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Shipping Method :
Shipped at Room temp
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Description
Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Introduction
CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.
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Synonyms
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human 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 Thymosin B4 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
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES
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 :
KLK13 HumanDescription:
Kallikrein-13 Human Recombinant
Kallikrein-13, KLK-L4, KLKL4, Kallikrein-like protein 4.
Product # :
ENZ-846Price :
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Shipped with Ice Packs
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Description
KLK13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (17-277 a.a) and having a molecular mass of 31.3kDa.KLK13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KLK13 protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.
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Synonyms
Kallikrein-13, KLK-L4, KLKL4, Kallikrein-like protein 4.
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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 MGSGGVSQES SKVLNTNGTS GFLPGGYTCF PHSQPWQAAL LVQGRLLCGG VLVHPKWVLT AAHCLKEGLK VYLGKHALGR VEAGEQVREV VHSIPHPEYR RSPTHLNHDH DIMLLELQSP VQLTGYIQTL PLSHNNRLTP GTTCRVSGWG TTTSPQVNYP KTLQCANIQL RSDEECRQVY PGKITDNMLC AGTKEGGKDS CEGDSGGPLV CNRTLYGIVS WGDFPCGQPD RPGVYTRVSR YVLWIRETIR KYETQQQKWL KGPQ.
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 :
HIV-1 p24, HisDescription:
HIV-1 p24 Recombinant, His Tag
Product # :
HIV-159Price :
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Shipped with Ice Packs
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Description
HIV-1 p24 His Tag Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (155-321 a.a.) and having a molecular mass of 21.2 kDa. The HIV-1 p24 is fused to a 21 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The HIV-1 p24 protein solution contains 20mM Tris-HCl pH-8, 0.1mM PMSF, 0.1M NaCl and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
The HIV1 p24 His Tag protein performs complex orchestrated tasks during the assembly, budding maturation and infection stages of the viral replication cycle. Throughout viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. HIV-1 P24 gag, the key capsid protein of the HIV-1 virion, is used in clinical trials as one of the components of the HIV-1 vaccine because of the great extent of sequence homology between different isolates.
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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 MWVKVVEEKA FSPEVIPMFS ALSEGATPQD LNTMLNTVGG HQAAMQMLKE TINEEAAEWD RLHPVHAGPI APGQMREPRG SDIAGTTSTL QEQIGWMTHN PPIPVGEIYK RWIILGLNKI VRMYSPTSIL DIRQGPKEPF RDYVDRFYKT LRAEQASQEV
KNWMTETL.
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 :
SEPT2 HumanDescription:
Septin-2 Human Recombinant
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
Product # :
PRO-255Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEPT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 381 amino acids (1-361 a.a.) and having a molecular mass of 43.6kDa. SEPT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEPT2 solution (0.25mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPT2 is a GTPase which is mandatory for cytokinesis and related to exocytosis. Septin-2 protein is able to hetero-oligomerize with Septin6, 7 and in addition takes part in the organization of new growth in organisms. SEPT2 is associated with a Tau-based paired helical filament core and contributes to the creation of neurofibrillary tangle as integral constituents of paired helical filaments.
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Synonyms
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
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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 MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT DLYPERVISG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH 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 :
p38a/SAPK2 HumanDescription:
p38a/SAPK2 Human Recombinant
Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.
Product # :
PKA-217Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
p38/SAPK2 is a non-glycosilated polypeptide produced by phosphorylation of the purified p38 alpha with MKK6 having a molecular mass of 42.7 kDa.
Source
Escherichia Coli.
Formulation
p38/SAPK2 is supplied in 25mM Tris-HCl, 150mM NaCl, 1mM DTT, 50% glycerol, pH 8.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
p38a/SAPK2 is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of this kinase include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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Synonyms
Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.
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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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Unit Definition
No protease activity detectable, specific activity is 2.357.900 U*/mg (*1 U = 1 pmol/min transferred to myelin basic protein at 30°C).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRYBA4 HumanDescription:
Crystallin Beta A4 Human Recombinant
Beta-crystallin A4, Beta-A4 crystallin, CRYBA4, MCOPCT4.
Product # :
HSP-048Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYBA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 24.5kDa.CRYBA4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYBA4 protein (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Beta-crystallin A4 (CRYBA4) is a member of the beta/gamma-crystallin family which are the dominant structural components of the vertebrate eye lens. Beta-crystallins construct aggregates of various sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. The CRYBA4 gene being a beta acidic group member is part of a gene cluster with beta-B1, beta-B2, and beta-B3.
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Synonyms
Beta-crystallin A4, Beta-A4 crystallin, CRYBA4, MCOPCT4.
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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 MTLQCTKSAG PWKMVVWDED GFQGRRHEFT AECPSVLELG FETVRSLKVL SGAWVGFEHA GFQGQQYILE RGEYPSWDAW GGNTAYPAER LTSFRPAACA NHRDSRLTIF EQENFLGKKG ELSDDYPSLQ AMGWEGNEVG SFHVHSGAWV CSQFPGYRGF QYVLECDHHS GDYKHFREWG SHAPTFQVQS IRRIQQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MIP 1b HumanDescription:
Macrophage Inflammatory Protein-1 Beta Human Recombinant (CCL4)
Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.
Product # :
CHM-276Price :
Quantity :
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Description
Macrophage Inflammatory Protein-1 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7620 Dalton. The CCL4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.More Info
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Introduction
Macrophage Inflammatory Proteins belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now also named CCL3 and CCL4. Both factors are produced by macrophages after they are stimulated with bacterial endotoxins. MIP-1a and MIP-1b activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. MIP-1a and MIP-1b induce synthesis and release of other pro-inflammatory cytokines such as interleukin-1 (IL-1), IL-6 and TNF-alpha from fibroblasts and macrophages. CCL3 and CCL4 genes are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Met-Gly-Ser.
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 :
NRG1 A HumanDescription:
Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
Product # :
CYT-736Price :
Quantity :
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Description
Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa. NRG1-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 6.0 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of > 2.5×104 units/mg.More Info
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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.
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Synonyms
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-A 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 NRG1-A 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
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.
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 :
MyoglobinDescription:
Myoglobin Human
Myoglobin, MB, PVALB, MGC13548.
Product # :
PRO-565Price :
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Description
Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa. Myoglobin is released from recently injured myocardial cells within a few hours of Infarction. Peak levels are reached more quickly than CK-MB or Troponin complex.
Source
Human Cardiac Tissues.
Formulation
The protein solution is in 0.05M phosphate buffer pH 7.5 containing 0.15M NaCl and 0.09% NaN3. Filtered through a 0.2µM membrane.
Purity
Greater than 96.0%.
More Info
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Introduction
Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.
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Synonyms
Myoglobin, MB, PVALB, MGC13548.
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Physical Appearance
Sterile Filtered red solution.
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Stability
Human Myoglobin should be stored at 2-8°C.
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Human Virus Test
Starting material donor tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
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 :
HIV-1 p24, BiotinDescription:
HIV-1 p24 Recombinant, Biotin Labeled
Product # :
HIV-106Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.coli derived 39 kDa biotin labeled recombinant protein is a non-glycosylated polypeptide chain, containing the HIV-1 p24 immunodominant regions, amino acids 77-436.The HIV-1 p24 Biotinylated is fused to beta-galactosidase (114 kDa) at the N-terminus.
Source
Escherichia Coli.
Formulation
8M Urea, 20mM Tris-HCl pH 8.0, 10mM b-mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Human immunodeficiency virus (HIV) is a retrovirusthat can lead to a condition in which the immune systembegins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the humanimmune systemsuch as helper T cells(specifically CD4+ T cells), macrophagesand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosisin infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytesthat recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunityis lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genomeis converted to double-stranded DNAby a virally encoded reverse transcriptasethat is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integraseso that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latentand the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.
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Physical Appearance
Sterile filtered colorless clear solution.
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Stability
HIV-1 p24 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HIV-1 p24 antigen is suitable for ELISA and Western blots, excellent antigen for early detection of HIV seroconvertors with minimal specificity problems.
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Specificity
Immunoreactive with all sera of HIV-1 infected individuals.
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 :
ATF1 HumanDescription:
Activating Transcription Factor-1 Human Recombinant
Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.
Product # :
PKA-019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ATF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-271 and having a molecular mass of 31.8kDa.ATF1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ATF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.
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Synonyms
Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.
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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 MGSHMEDSHK STTSETAPQP GSAVQGAHIS HIAQQVSSLS ESEESQDSSD SIGSSQKAHG ILARRPSYRK ILKDLSSEDT RGRKGDGENS GVSAAVTSMS VPTPIYQTSS GQYIAIAPNG ALQLASPGTD GVQGLQTLTM TNSGSTQQGT TILQYAQTSD GQQILVPSNQ VVVQTASGDM QTYQIRTTPS ATSLPQTVVM TSPVTLTSQT TKTDDPQLKR EIRLMKNREA ARECRRKKKE YVKCLENRVA VLENQNKTLI EELKTLKDLY SNKSV
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 :
PLAUR HumanDescription:
PLAUR Human Recombinant
PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.
Product # :
PRO-2340Price :
Quantity :
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Shipped with Ice Packs
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Description
PLAUR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (23-305 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa).PLAUR is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PLAUR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PLAUR is one of 2 activators which convert the extracellular zymogen plasminogen to plasmin, a serine protease involved in a various normal and pathological processes that require cell migration and/or tissue destruction. PLAUR protein is synthesized and released from cells as a single-chain proenzyme with narrow enzymatic activity and is converted to an active two-chain disulfide-linked active enzyme by plasmin and other specific proteinases.
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Synonyms
PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.
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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
LRCMQCKTNG DCRVEECALG QDLCRTTIVR LWEEGEELEL VEKSCTHSEK TNRTLSYRTG LKITSLTEVV CGLDLCNQGN SGRAVTYSRS RYLECISCGS SDMSCERGRH QSLQCRSPEE QCLDVVTHWI QEGEEGRPKD DRHLRGCGYL PGCPGSNGFH NNDTFHFLKC CNTTKCNEGP ILELENLPQN GRQCYSCKGN STHGCSSEET FLIDCRGPMN QCLVATGTHE PKNQSYMVRG CATASMCQHA HLGDAFSMNH IDVSCCTKSG CNHPDLDVQY RSGLEHHHHH 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.
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Name :
Resistin RatDescription:
Resistin Rat Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1129Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin 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 Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.
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 :
VWA2 HumanDescription:
Von Willebrand Factor A Domain Containing 2 Human Recombinant
A domain-containing protein similar to matrilin and collagen, AMACO, Colon cancer secreted protein 2, CCSP-2.
Product # :
PRO-2752Price :
Quantity :
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Shipped with Ice Packs
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Description
VWA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (341-517 a.a) and having a molecular mass of 19.3kDa.The VWA2 is expressed with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VWA2 protein solution contains 20mM Tris-HCl, pH 8.0, 0.8M Urea & 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Von Willebrand Factor A Domain Containing 2 (VWA2) is an extracellular matrix protein containing vWA-like domains. VWA2 contains a signal peptide sequence, an N-terminal VWA domain connected to 2 additional tandem vWA domains by a cysteine-rich sequence and an EGF-like domain. Also, another EGF-like domain is located at the C-terminus. Expression of VWA2 is induced in stage II, III and IV colon cancers and colon adenomas and is considered a novel serum marker for the diagnosis of early-stage colon cancer.
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Synonyms
A domain-containing protein similar to matrilin and collagen, AMACO, Colon cancer secreted protein 2, CCSP-2.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACOT11 AntibodyDescription:
Acyl-Coenzyme A Thioesterase 11, Mouse Anti Human
Acyl-coenzyme A thioesterase 11, Acyl-CoA thioesterase 11, Acyl-CoA thioester hydrolase 11, Brown fat-inducible thioesterase, BFIT, Adipose-associated thioesterase, ACOT11, BFIT, KIAA0707, THEA, BFIT1, BFIT2, THEM1, STARD14.
Product # :
ANT-424Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide & 10% Glycerol.
More Info
-
Introduction
ACOT11 is a protein with acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Expression of a similar murine protein in brown adipose tissue is induced by cold exposure and repressed by warmth. Expression of the mouse ACOT11 has been linked to obesity, with higher expression found in obesity-resistant mice compared with obesity-prone mice.
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Synonyms
Acyl-coenzyme A thioesterase 11, Acyl-CoA thioesterase 11, Acyl-CoA thioester hydrolase 11, Brown fat-inducible thioesterase, BFIT, Adipose-associated thioesterase, ACOT11, BFIT, KIAA0707, THEA, BFIT1, BFIT2, THEM1, STARD14.
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Immunogen
Anti-human ACOT11 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ACOT11 amino acids 19-250 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PJ4B2AT.
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Applications
ACOT11 antibody has been tested by ELISA, Western blot and immunohistochemistry 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 is 1:500 ~ 1:2,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:100.
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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
ACOT11 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 :
AICDA AntibodyDescription:
Activation-induced cytidine deaminase, Mouse Anti Human
Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.
Product # :
ANT-411Price :
Quantity :
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Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
AICDA is an RNA-editing deaminase which belongs to the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination of immunoglobulin genes. Defects in the AICDA gene are the cause of autosomal recessive hyper-IgM immunodeficiency syndrome type 2 (HIGM2).
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Synonyms
Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.
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Immunogen
Anti-human AICDA mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human AICDA amino acids 1-54 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P2D3AT.
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Applications
AICDA 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
AICDA 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 :
LanreotideDescription:
Lanreotide
Product # :
HOR-282Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lanreotide is an octapeptide, an analogue of a naturally occurring hormone, somatostatin.
Formulation
The protein (1mg/ml) was lyophilized with 5mg manntitol and 0.04mg tween-80.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Lanreotide is a peptide inhibitor of a number of endocrine, neuroendocrine, exocrine and paracrine functions. It shows good affinity for peripheral somatostatin receptors (anterior pituitary and pancreatic). In contrast, its affinity for central receptors is much lower. This profile confers a good specificity of action at the level of growth hormone and digestive hormone secretion. Lanreotide shows a much longer duration of action than natural somatostatin. In addition, its marked selectivity for the secretion of growth hormone, compared to that of insulin, makes it a suitable candidate for the treatment of acromegaly. By inhibiting the synthesis of thyroid stimulating hormone (TSH), lanreotide also normalised thyroid function of patients with thyrotrophin secreting adenomas in 50% (8/16) of the per-protocol population treated for 6 months. There was no significant reduction in the size of the adenoma. Furthermore, the inhibitory action of lanreotide on intestinal exocrine secretion, d
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Lanreotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lanreotide 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 Lanreotide in sterile 18MΩ-cm H2O not less than 100 µg/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 :
Leptin qA Mouse, PEGDescription:
Leptin Quadruple Antagonist Pegylated Mouse Recombinant
Product # :
CYT-1244Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PSIP1 HumanDescription:
PC4 And SFRS1 Interacting Protein 1 Human Recombinant
PC4 and SFRS1 Interacting Protein 1, Lens Epithelium-Derived Growth Factor, Transcriptional Coactivator P75/P52, Dense Fine Speckles 70 KDa Protein, CLL-Associated Antigen KW-7, DFS 70, PSIP2, DFS70, LEDGF, PC4 And SFRS1 Interacting Protein 2, Transcriptional Coactivator P52/P75, PAIP, P52, P75, PSIP1.
Product # :
PRO-2267Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human PSIP1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 71 kDa. PSIP1 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PSIP1 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 84.0% as determined by SDS-PAGE.
More Info
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Introduction
PC4 and SFRS1 Interacting Protein 1 (PSIP1) is a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. PSIP1 is also involved particularly in lens epithelial cell gene regulation and stress responses. PSIP1 has a significant role in lens epithelial to fiber cell terminal differentiation. In addition, PSIP1 plays a protective role during stress-induced apoptosis. Furthermore, PSIP1 is a cellular cofactor for lentiviral integration.
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Synonyms
PC4 and SFRS1 Interacting Protein 1, Lens Epithelium-Derived Growth Factor, Transcriptional Coactivator P75/P52, Dense Fine Speckles 70 KDa Protein, CLL-Associated Antigen KW-7, DFS 70, PSIP2, DFS70, LEDGF, PC4 And SFRS1 Interacting Protein 2, Transcriptional Coactivator P52/P75, PAIP, P52, P75, PSIP1.
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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 Functions
1. Binds IgG type human auto-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.