Search: 1000 results found for "avidin"

Description:

Nectin Cell Adhesion Molecule 3 Human Recombinant

Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.

Product # :

PRO-2504

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Description

NECTIN3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 355 amino acids (58-404 a.a.) and having a molecular mass of 39.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

NECTIN3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NECTIN3, also known as Nectin Cell Adhesion Molecule 3, is part of the nectin family. NECTIN3 is intended to initiate cell-cell adhesion to stimulate cell attachment and to allow subsequent formation of JAM-and cadherin-based intercellular junctions. NECTIN3 induces endocytosis-mediated down-regulation of PVR from the cell surface, which results in reduction of cell movement & proliferation. Following Nectin-3 activity adds strength to the junction through trans-interaction with various molecules.
Synonyms
Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.
Physical Appearance
Sterile filtered colorless solution.
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.
Amino Acid Sequence
GPIIVEPHVT AVWGKNVSLK CLIEVNETIT QISWEKIHGK SSQTVAVHHP QYGFSVQGEY QGRVLFKNYS LNDATITLHN IGFSDSGKYI CKAVTFPLGN AQSSTTVTVL VEPTVSLIKG PDSLIDGGNE TVAAICIAAT GKPVAHIDWE GDLGEMESTT TSFPNETATI ISQYKLFPTR FARGRRITCV VKHPALEKDI RYSFILDIQY APEVSVTGYD GNWFVGRKGV NLKCNADANP PPFKSVWSRL DGQWPDGLLA SDNTLHFVHP LTFNYSGVYI CKVTNSLGQR SDQKVIYISD PPTTTTLQPT IQWHPSTADI EDLATEPKKL PFPLSTLATI KDDTIATLEH HHHHH.

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.

Description:

Vesicle Transport Through Interaction with t-SNAREs Homolog 1B Human Recombinant

Vesicle transport through interaction with t-SNAREs homolog 1B, Vesicle transport v-SNARE protein Vti1-like 1, Vti1-rp1, VTI1B, VTI1, VTI1L, VTI1L1, VTI2, v-SNARE, VTI1-LIKE.

Product # :

PRO-1115

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Description

VTI1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.3kDa (Molecular weight on SDS-PAGE will appear higher).VTI1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VTI1B protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
VTI1B (v-SNARE) mediates vesicle transport pathways via interactions with t-SNAREs on the target membrane. These interactions are meant to facilitate aspects of the specificity of vesicle trafficking and to stimulate fusion of the lipid bilayers. VTI1B may be involved in increased secretion of cytokines connected with cellular senescence.
Synonyms
Vesicle transport through interaction with t-SNAREs homolog 1B, Vesicle transport v-SNARE protein Vti1-like 1, Vti1-rp1, VTI1B, VTI1, VTI1L, VTI1L1, VTI2, v-SNARE, VTI1-LIKE.
Physical Appearance
Sterile Filtered colorless solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASSAAS SEHFEKLHEI FRGLHEDLQG VPERLLGTAG TEEKKKLIRD FDEKQQEANE TLAEMEEELR YAPLSFRNPM MSKLRNYRKD LAKLHREVRS TPLTATPGGR GDMKYGIYAV ENEHMNRLQS QRAMLLQGTE SLNRATQSIE RSHRIATETD QIGSEIIEEL GEQRDQLERT KSRLVNTSEN LSKSRKILRS MSRKVTTNKL L.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thymidine Kinase 1 Human Recombinant

Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

Product # :

PKA-036

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Description

TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.
Synonyms
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
Physical Appearance
Sterile Filtered colorless solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

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.

Description:

Leptin Chicken Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-505

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Description

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 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 calibrated solution of Leptin Chicken 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.

Description:

Adenosine Kinase, Mouse Anti Human

Adenosine 5''-phosphotransferase, EC 2.7.1.20, AK, ADK.

Product # :

ANT-057

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.
Synonyms
Adenosine 5''-phosphotransferase, EC 2.7.1.20, AK, ADK.
Immunogen
Anti-human ADK mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ADK amino acids 22-362 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT4F8AT.
Applications
ADK 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 1:1000.
Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
ADK 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.

Description:

Gliadin Gamma 18.6kD Wheat Recombinant

Product # :

PRO-114

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Description

Gliadin is a cDNA coding for an epitope-carrying fragment of a wheat gamma-gliadin isoform, having a molecular mass of 19 kDa (high proline content and the low pI are likely causes for the observed discrepancy between calculated molecular weight and the observed electrophoretic mobility of approx. 50 kDa on standard SDS-PAGE), pH 4.6. By sequence design the epitopes correspond to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation. Gliadin protein is fused to a hexa-histidine purification tag.

Source

Escherichia Coli.

Formulation

Gliadin is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl, and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
Physical Appearance
Sterile Filtered clear solution.
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.
Immunological Functions
1. Binds IgG- and IgA-type human autoantibodies associated with celiac disease. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot.
coating concentration
0.15-0.5 µg/ml (depending on the type of ELISA plate and coating buffer).
Applications
Western blot with monoclonal anti-hexa-His-tag antibody.

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.

Description:

Apolipoprotein E4 Human Recombinant

Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.

Product # :

CYT-968

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Description

Apolipoprotein E4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 299 amino acids and having a molecular mass of 34.4kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 20mM PBS, pH7.8 and 5% trehalose.

Purity

Greater than 95% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

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Introduction
Apolipoprotein E (APOE) is a chylomicron lipoprotein which is essential for the metabolism of lipoproteins and lipid transport. The APOE gene has 3 alleles, designated APOE2, APOE3, and APOE4. The APOE allelic proteins differ by only one or two amino acids, however have different biological structures and functions. APOE3 is the most common and neutral allele. The APOE4 allele is linked with an increased risk for Alzheimer's Disease (AD) and coronary artery disease (CAD). The APOE4 protein morphology decreases the ability of APOE4 to clear beta-amyloid protein from the brain, resulting in AD progression. The APOE2 allele is linked with type III hyperlipoproteinemia, which is characterized by defects in the clearance of plasma lipoproteins, however APOE2 may have a protective effect against AD.
Synonyms
Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized APOE4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOE4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized APOE4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.
Background
What is the molecular weight/Mw of APOE4 Protein?
APOE4 Protein has a total Mw of 34.4kDa.

What is the source or expression system of APOE4 Protein?
Escherichia Coli.

What is the Purity of APOE4 Protein?
APOE4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of APOE4 Protein?
When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

What is the amino acid sequence of APOE4 Protein?
KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.

What applications can APOE4 Protein be used in?
APOE4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOE4 Protein?
The endotoxin level is minimal, APOE4 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.

Description:

Secretin Human

Product # :

HOR-273

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Description

Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Secretin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secretin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Secretin 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.

Description:

Inhibin-Alpha A Chain Human Recombinant

Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

Product # :

HOR-293

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Description

Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
Synonyms
Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.
Physical Appearance
Sterile Filtered clear solution.
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.
Background
What is the molecular weight/Mw of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein has a total Mw of 19.2kDa.

What is the source or expression system of INHIBIN ALPHA Protein?
Escherichia Coli.

What is the Purity of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of INHIBIN ALPHA Protein?
The biological functionality of INHIBIN ALPHA Protein will be determined in the future.

What is the amino acid sequence of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein is composed from 134 amino acids.

What applications can INHIBIN ALPHA Protein be used in?
INHIBIN ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for INHIBIN ALPHA Protein?
The endotoxin level is minimal, INHIBIN ALPHA Protein was purified using conventional chromatography techniques.

Who supplies recombinant INHIBIN ALPHA 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 INHIBIN ALPHA?
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.

Description:

Apolipoprotein-M Human Recombinant

G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

Product # :

CYT-715

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Description

APOM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (23-188 a.a.) and having a molecular mass of 20.9 kDa. APOM protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

APOM Human solution containing 20mM Tris-HCl pH-8 1mM DTT & 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport. .
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
Physical Appearance
Sterile filtered colorless solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.
Background
Apolipoprotein-M Human Recombinant: Insights into its Role in Lipid Metabolism and Cardiovascular Health
Abstract:

Apolipoprotein-M (ApoM), a unique member of the apolipoprotein family, has gained significant attention in the field of lipid metabolism and cardiovascular health. This research paper provides a comprehensive analysis of ApoM human recombinant, exploring its structure, function, and potential implications in cardiovascular diseases. Understanding the intricate nature of ApoM sheds light on its significance as a potential biomarker and therapeutic target in cardiovascular disorders. This article presents a concise yet comprehensive examination of ApoM, highlighting its impact on human health.
Introduction:

Cardiovascular diseases remain a leading cause of global morbidity and mortality, underscoring the importance of understanding lipid metabolism and its association with cardiovascular health. ApoM, an intriguing apolipoprotein, has emerged as a key player in lipid metabolism and cardiovascular function. This paper delves into the intricate nature of ApoM, elucidating its structure, molecular interactions, and potential roles in cardiovascular diseases.
Structure and Function of Apolipoprotein-M:

ApoM exhibits a unique structural configuration, comprising a single membrane-bound alpha-helix and a lipocalin-like domain. It predominantly associates with high-density lipoproteins (HDL) and plays a critical role in HDL metabolism and cholesterol transport. Additionally, ApoM has been implicated in endothelial function, inflammation, and modulation of sphingolipid metabolism.
Apolipoprotein-M and Cardiovascular Diseases:

Studies have highlighted the potential involvement of ApoM in cardiovascular diseases, such as atherosclerosis and coronary artery disease. Genetic variations in the ApoM gene and alterations in ApoM levels have been associated with disease development and progression. Understanding the role of ApoM in cardiovascular diseases offers insights into potential therapeutic interventions and diagnostic strategies.
Apolipoprotein-M Human Recombinant Production:

The production of ApoM human recombinant is made possible through advanced biotechnological techniques, including recombinant DNA technology and protein expression systems. These methods facilitate large-scale production, purification, and characterization of ApoM, providing opportunities for further research and potential therapeutic applications.
Therapeutic Potential of Apolipoprotein-M Human Recombinant:

Exploring the therapeutic potential of ApoM holds promise in the field of cardiovascular disorders. Strategies aimed at modulating ApoM expression or function may contribute to the prevention or treatment of lipid metabolism-related diseases. Furthermore, ApoM may serve as a potential biomarker for risk assessment and monitoring of cardiovascular conditions.
Conclusion:

Apolipoprotein-M human recombinant represents a fascinating area of research, shedding light on the role of this protein in lipid metabolism and cardiovascular health. Understanding the structure, function, and genetic implications of ApoM is pivotal in advancing our knowledge and exploring its potential as a therapeutic target. Continued investigation into the mechanisms and signaling pathways involving ApoM will likely pave the way for innovative strategies in the diagnosis, prevention, and treatment of cardiovascular diseases.
What is the molecular weight/Mw of APOM Protein?
APOM Protein has a total Mw of 20.9kDa.

What is the source or expression system of APOM Protein?
Escherichia Coli.

What is the Purity of APOM Protein?
APOM Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of APOM Protein?
The biological functionality of APOM Protein will be determined in the future.

What is the amino acid sequence of APOM Protein?
MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.

What applications can APOM Protein be used in?
APOM Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOM Protein?
The endotoxin level is minimal, APOM 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.

Description:

Leptin Antagonist Triple Mutant Ovine Recombinant

Product # :

CYT-356

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Quantity :

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Description

Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin 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.
Solubility
It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 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.

Description:

Coronavirus 2019 Nucleocapsid (1-419 a.a.), Biotinylated Recombinant

Product # :

SARS-036

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Description

The HEK293 derived recombinant biotinylated protein contains the Coronavirus 2019 CoV-2 Nucleocapsid, Wuhan-Hu-1 strain, amino acids 1-419 fused to His-Avi tag at C-terminal.

Source

HEK293 Cells.

Formulation

CoV-2 Nucleocapsid protein is supplied in 50mM Tris, 0.15M NaCl & Arginine, pH7.5

Purity

Protein is >90% pure as determined SDS-PAGE.

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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cov-2 Nucleocapsid protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Nucleocapsid protein 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.
Purification Method
Purified by Metal-Afinity chromatographic technique.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Resistin Mutant Human Recombinant

Resistin, 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-585

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Description

9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.

Source

Escherichia Coli.

Formulation

Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
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
Resistin, 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.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.

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.

Description:

Alcohol Dehydrogenase 6 Human Recombinant

Alcohol dehydrogenase 6, ADH6, ADH-5.

Product # :

ENZ-619

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADH6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Alcohol dehydrogenase 6 (ADH6) belongs to the alcohol dehydrogenase family. Alcohol dehydrogenase family members metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH6 is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5’ UTR, which is a steroid hormone receptor binding site.
Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
Physical Appearance
Sterile Filtered colorless solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTTGQ VIRCKAAILW KPGAPFSIEE VEVAPPKAKE VRIKVVATGL CGTEMKVLGS KHLDLLYPTI LGHEGAGIVE SIGEGVSTVK PGDKVITLFL PQCGECTSCL NSEGNFCIQF KQSKTQLMSD GTSRFTCKGK SIYHFGNTST FCEYTVIKEI SVAKIDAVAP LEKVCLISCG FSTGFGAAIN TAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIGVDVN KEKFKKAQEL GATECLNPQD LKKPIQEVLF DMTDAGIDFC FEAIGNLDVL AAALASCNES YGVCVVVGVL PASVQLKISG QLFFSGRSLK GSVFGGWKSR QHIPKLVADY MAEKLNLDPL ITHTLNLDKI NEAVELMKTG KCIRCILLL.

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.

Description:

ADP-Ribosylation Factor 5 Human Recombinant

ADP-ribosylation factor 5, ARF5.

Product # :

PRO-245

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Quantity :

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Description

ARF5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (1-180 a.a) and having a molecular mass of 22.6kDa.ARF5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ARF5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ADP-ribosylation factor 5 (ARF5) is a small guanine nucleotide-binding protein which enhances the enzymatic activities of cholera toxin. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the connection of actin to the golgi via rho family-dependent G-protein localization and WASP/Arp2/3 complexes. ARF5 is involved in vesicular transport and functioning via phospholipase D activation.
Synonyms
ADP-ribosylation factor 5, ARF5.
Physical Appearance
Sterile filtered colorless solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA
TQGTGLYDGL DWLSHELSKR.

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.

Description:

Embryonic Ectoderm Development Human Recombinant

Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.

Product # :

PRO-1503

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Description

EED Human Recombinant produced in E. coli is a single polypeptide chain containing 464 amino acids (1-441) and having a molecular mass of 52.6kDa. EED is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EED solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
EED is a part of the Polycomb-group family whose members form multimeric protein complexe that are involved in preserving the transcriptional repressive state of genes over successive cell generations. EED mediates repression of gene activity through histone deacetylation, and acts as a specific regulator of integrin function. EED protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin ?7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins.
Synonyms
Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.
Physical Appearance
Sterile Filtered clear solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEREVS TAPAGTDMPA AKKQKLSSDE NSNPDLSGDE NDDAVSIESG TNTERPDTPT NTPNAPGRKS WGKGKWKSKK CKYSFKCVNS LKEDHNQPLF GVQFNWHSKE GDPLVFATVG SNRVTLYECH SQGEIRLLQS YVDADADENF YTCAWTYDSN TSHPLLAVAG SRGIIRIINP ITMQCIKHYV GHGNAINELK FHPRDPNLLL SVSKDHALRL WNIQTDTLVA IFGGVEGHRD EVLSADYDLL GEKIMSCGMD HSLKLWRINS KRMMNAIKES YDYNPNKTNR PFISQKIHFP DFSTRDIHRN YVDCVRWLGD LILSKSCENA IVCWKPGKME DDIDKIKPSE SNVTILGRFD YSQCDIWYMR FSMDFWQKML ALGNQVGKLY VWDLEVEDPH KAKCTTLTHH KCGAAIRQTS FSRDSSILIA VCDDASIWRW DRLR.

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.

Description:

Thioredoxin Human Recombinant, His Tag

Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

Product # :

PRO-804

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Description

Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

TXN1 solution containing 1x PBS pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Physical Appearance
Sterile filtered colorless solution.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.

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.

Description:

Apolipoprotein-J Human Recombinant, His Tag

CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

Product # :

CYT-814

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sds-page
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Description

Clusterin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 463 amino acids (23-449 a.a.) and having a molecular mass of 54.1kDa. Clusterin is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Clusterin protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.
Synonyms
CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.
Physical Appearance
Sterile filtered colorless solution.
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.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.
Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 54.1kDa.

What is the source or expression system of CLUSTERIN Protein?
Escherichia Coli.

What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.

What is the amino acid sequence of CLUSTERIN Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN 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.

Description:

Resistin Human Recombinant, His Tag

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-256

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
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.
Physical Appearance
Sterile filtered colorless solution.
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.

Description:

Leptin Rabbit Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-507

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Leptin Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.505 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.

Description:

Nafarelin Acetate

Product # :

HOR-248

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Shipped at Room temp

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Description

Nafarelin is a decapeptide containing 9 amino acids Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.Nafarelin is purified by proprietary chromatographic techniques.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Nafarelin acetate is a synthetic analog of the naturally occurring gonadotropin-releasing hormone (GnRH). Nafarelin stimulates the release of the pituitary gonadotropins, LH and FSH, resulting in a temporary increase of ovarian steroidogenesis.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Nafarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NAF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Nafarelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.
Background
What is the Purity of NAFARELIN Protein?
NAFARELIN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of NAFARELIN Protein?
The biological functionality of NAFARELIN Protein will be determined in the future.

What is the amino acid sequence of NAFARELIN Protein?
Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.

What applications can NAFARELIN Protein be used in?
NAFARELIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for NAFARELIN Protein?
The endotoxin level is minimal, NAFARELIN Protein was purified using conventional chromatography techniques.

Who supplies NAFARELIN 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 NAFARELIN?
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.

Description:

LL-37

LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.

Product # :

HOR-041

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Shipped at Room temp

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Description

LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Synonyms
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized LL-37 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.
Background
LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.
LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.
LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).
LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).
LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).
The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).
LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.

What is the molecular weight/Mw of LL-37 Protein?
LL-37 Protein has a total Mw of 4.493kDa.

What is the Purity of LL-37 Protein?
LL-37 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of LL-37 Protein?
The biological functionality of LL-37 Protein will be determined in the future.

What is the amino acid sequence of LL-37 Protein?
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.

What applications can LL-37 Protein be used in?
LL-37 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LL-37 Protein?
The endotoxin level is minimal, LL-37 Protein was purified using conventional chromatography techniques.

Who supplies LL-37 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 LL-37?
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.

Description:

Visfatin, Mouse Anti Human

PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

Product # :

ANT-368

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Shipped with Ice Packs

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Formulation

1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.

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Introduction
Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-α, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It h
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Immunogen
Anti-human Visfatin mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Visfatin amino acids 1-491 purified from E. coli.
Ig Subclass
Mouse IgG1heavy chain and κ light chain.
Clone
P4D5AT.
Applications
Visfatin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Visfatin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Humanin

Product # :

HOR-042

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Shipped at Room temp

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Description

Humanin Synthetic is a single, non-glycosylated polypeptide chain containing 24 amino acids, having a molecular mass of 2687 Dalton and a Molecular formula of C119H204N34O32S2 .

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Humanin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Humanin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Humanin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.
Background
Humanin, a small peptide derived from the mitochondrial genome, has emerged as a remarkable molecule with diverse cellular protective functions. This research paper aims to provide a comprehensive analysis of Humanin, exploring its biochemical properties, mechanisms of action, and potential therapeutic applications in various disease contexts.
Humanin, initially discovered for its role in neuroprotection, has since garnered interest for its broad spectrum of cytoprotective effects. Derived from the mitochondrial 16S ribosomal RNA, this small peptide plays a critical role in safeguarding cells from various stressors (Harvey, 2008). This paper delves into the complexities of Humanin, uncovering its multifaceted nature and potential clinical applications.
Humanin is a 24-amino acid peptide with a unique secondary structure that contributes to its cellular protective functions. It localizes to both the cytoplasm and mitochondria, where it interacts with various proteins involved in apoptotic and oxidative stress pathways (Hoang et al., 2019). Additionally, Humanin can undergo post-translational modifications, further diversifying its actions.
Humanin exerts its protective effects through multiple mechanisms. It interacts with the pro-apoptotic protein Bax, inhibiting its translocation to the mitochondria and preventing the release of cytochrome c (Hashimoto et al., 2001). Humanin also modulates the activities of caspases, key mediators of cell death pathways, thereby promoting cell survival in stressful conditions (Nakagawa et al., 2002).
Beyond its initial recognition as a neuroprotective agent, Humanin has demonstrated cytoprotective effects in various cell types, including cardiomyocytes, neurons, and endothelial cells (Chai et al., 2019). It attenuates oxidative stress, reduces mitochondrial dysfunction, and promotes cell viability, thereby safeguarding cells from a multitude of insults.
The multifaceted protective functions of Humanin offer promising therapeutic potential in various disease contexts. Research has shown its efficacy in mitigating neurodegenerative disorders, cardiovascular diseases, and age-related pathologies (Muzumdar et al., 2009). Furthermore, Humanin's ability to attenuate inflammation and promote tissue repair opens new avenues for therapeutic interventions.

What is the molecular weight/Mw of HUMANIN Protein?
HUMANIN Protein has a total Mw of 2.687kDa.

What is the Purity of HUMANIN Protein?
HUMANIN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of HUMANIN Protein?
The biological functionality of HUMANIN Protein will be determined in the future.

What is the amino acid sequence of HUMANIN Protein?
H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.

What applications can HUMANIN Protein be used in?
HUMANIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HUMANIN Protein?
The endotoxin level is minimal, HUMANIN Protein was purified using conventional chromatography techniques.

Who supplies HUMANIN 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 HUMANIN?
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.

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