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Description:

Apolipoprotein C-I Human Recombinant

Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.

Product # :

CYT-812

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Description

APOC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids (27-83 a.a.) and having a molecular mass of 9.0kDa. APOC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APOC1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

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Introduction
Apolipoprotein C-I (APOC1) which expressed mainly in the liver is a part of the apolipoprotein C family. APOC1 which is usually found in plasma and responsible for the activation of esterified lechitin cholesterol takes an important part in the exchange of esterified cholesterol among lipoproteins and in removal of cholesterol from tissues. APOC1 is activated when monocytes differentiate into macrophages. APOC1 protein’s main role is to inhibit CETP by altering the electric charge of HDL molecules. APOC1 is also binds free fatty acids and reduces their intracellular esterification.
Synonyms
Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.
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 MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.
Background
Apolipoprotein C-I Human Recombinant: Unraveling the Complexity of Lipid Regulation
Abstract:
Apolipoprotein C-I (ApoC-I) is a remarkable protein that plays a significant role in lipid metabolism and cardiovascular health. It is primarily synthesized in the liver and is associated with lipoproteins involved in lipid transport. This research paper aims to provide a comprehensive overview of ApoC-I human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications. By delving into the intricacies of ApoC-I, we can gain valuable insights into its role as a key player in lipid regulation and its potential as a therapeutic target.
Introduction:
The prevalence of lipid disorders and cardiovascular diseases necessitates a deeper understanding of the mechanisms governing lipid metabolism. ApoC-I, a critical component of lipoproteins, offers unique insights into the regulation of lipid levels and its implications for cardiovascular health.
Structure and Function of Apolipoprotein C-I:
ApoC-I exhibits a complex molecular structure, comprising functional domains that enable its interaction with lipoproteins. It plays a crucial role in regulating lipoprotein metabolism by inhibiting the activity of lipoprotein lipase and modulating the clearance of triglyceride-rich lipoproteins.
Regulation of Apolipoprotein C-I Expression:
The synthesis and secretion of ApoC-I are tightly regulated processes influenced by various factors, including nutritional status and hormonal signals. Understanding the regulatory mechanisms underlying ApoC-I expression can provide insights into its role in maintaining lipid homeostasis.
Apolipoprotein C-I and Cardiovascular Diseases:
Dysregulation of ApoC-I has been associated with various lipid disorders and cardiovascular diseases. Altered levels of ApoC-I have been observed in conditions such as hypertriglyceridemia and atherosclerosis, highlighting its potential as a biomarker for cardiovascular risk assessment.
Production of Apolipoprotein C-I Human Recombinant:
Recombinant ApoC-I can be produced using advanced biotechnological approaches, including recombinant DNA technology and protein expression systems. These methods enable large-scale production, purification, and characterization of ApoC-I, facilitating its potential therapeutic applications.
Therapeutic Potential of Apolipoprotein C-I Human Recombinant:
Targeting ApoC-I opens up exciting avenues for therapeutic interventions in lipid disorders and cardiovascular diseases. Modulating ApoC-I expression or function holds promise for restoring lipid balance and reducing the risk of cardiovascular complications.
Conclusion:
Apolipoprotein C-I human recombinant represents a fascinating area of research in the field of lipid metabolism and cardiovascular health. By unraveling the intricate interplay between ApoC-I, lipoproteins, and cardiovascular diseases, we can pave the way for novel therapeutic strategies and improved risk assessment. Further studies are required to fully understand the therapeutic potential of ApoC-I human recombinant and translate these findings into clinical applications.
What is the molecular weight/Mw of APOC1 Protein?
APOC1 Protein has a total Mw of 9kDa.

What is the source or expression system of APOC1 Protein?
Escherichia Coli.

What is the Purity of APOC1 Protein?
APOC1 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of APOC1 Protein?
The biological functionality of APOC1 Protein will be determined in the future.

What is the amino acid sequence of APOC1 Protein?
MGSSHHHHHH SSGLVPRGSH MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.

What applications can APOC1 Protein be used in?
APOC1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOC1 Protein?
The endotoxin level is minimal, APOC1 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:

Apolipoprotein-D Human Recombinant, HEK

Apolipoprotein D, Apo-D, ApoD.

Product # :

CYT-768

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Description

Apolipoprotein-D Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 21-189) containing a total of 175 amino acids, having a molecular mass of 20.1kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human APOD is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue.
Synonyms
Apolipoprotein D, Apo-D, ApoD.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.
Background
What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 20.1kDa.

What is the source or expression system of APO D Protein?
HEK 293.

What is the Purity of APO D Protein?
APO D Protein is >80% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of APO D Protein?
QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.

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

What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D 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:

Hemoglobin, Alpha 2 Human Recombinant

Hemoglobin alpha chain, hemoglobin alpha 2, hemoglobin subunit alpha, Alpha-globin, alpha-2 globin, HBH.

Product # :

PRO-1183

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Description

HBA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 179 amino acids (1-142) and having a molecular mass of 19.5 kDa.HBA2 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The HBA2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 2M urea and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
HBA2 is a member of the globin family. HBA2 takes part in oxygen transport from the lung to the different peripheral tissues. The coding sequences of HBA2 and HBA1 are equal but have a small difference over the 5' untranslated regions and the introns, and a large difference over the 3' untranslated regions. HbA is constituted from two alpha chains and two beta chains which in standard adult life hold about 97% of the total hemoglobin; alpha chains associate with delta chains to create HbA-2 that with HbF (fetal hemoglobin) form the remaining 3% of adult hemoglobin. Alpha thalassemia is caused by removal of each of the alpha genes or removal of both HBA2 and HBA1; nondeletion alpha thalassemias has also been reported.
Synonyms
Hemoglobin alpha chain, hemoglobin alpha 2, hemoglobin subunit alpha, Alpha-globin, alpha-2 globin, HBH.
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 KDRWGSHMVL SPADKTNVKA AWGKVGAHAG EYGAEALERM FLSFPTTKTY FPHFDLSHGS AQVKGHGKKV ADALTNAVAH VDDMPNALSA LSDLHAHKLR VDPVNFKLLS HCLLVTLAAH LPAEFTPAVH ASLDKFLASV STVLTSKYR

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:

Crystallin Alpha B Human Recombinant

CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

Product # :

HSP-003

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Description

Recombinant CRYAB produced in E.Coli is a single,non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.1kDa. CRYAB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRYAB protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH-7.5, 50mM NaCl and 1mM EDTA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSWFDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHRKYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK.

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 Antagonist Human 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-1255

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Description

Resistin Human antagonist is a monomeric C7A mutant that does not form covalent dimers. Resistin Human antagonist is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

Resistin was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Analysis by Gel Filtration.

(b) Analysis by SDS-PAGE.

(c) Analysis by RP-HPLC.

Biological Activity

The biological activity was evidenced by resistin antagonist activity to inhibit resistin-induced Akt phosphorylation in two cell lines. It also reduced the weight (mainly the visceral fat) and normalized GTT and ITT inHFD-fed mice.

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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 White lyophilized (freeze-dried) powder.
Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first seven N-terminal amino acids was determined and was found to be Ala-Ser-Ser-Lys-Thr-Leu-Ala.
Background
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis. Resistin blocks insulin stimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of low-density lipoprotein (LDL), increasing the risk of heart disease.

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:

Annexin A1 Human Recombinant

ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

Product # :

PRO-679

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Description

ANXA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-346 a.a.) and having a molecular mass of 38.7 kDa.ANXA1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ANXA1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.
Synonyms
ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.
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
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK
PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKCATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN.

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:

Angiotensin Converting Enzyme 2 (18-740 a.a.), Biotinylated Human Recombinant

Product # :

ENZ-1127

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Description

The HEK293 derived ACE2 Human recombinant biotinylated protein contains the amino acids Gln 18-Ser 740 fused to His-AVI tag at C-terminal having a predicted Mw of 87.2 kDa ( migrates 95-125 kDa under reducing conditions on sds-page due to glycosilation). ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.

Source

HEK293 Cells

Formulation

ACE2 Human protein solution is supplied in 50mM Tris, pH7.5, 150mM NaCl and 20% glycerol.

Purity

ACE-2 Protein is >90% pure as determined SDS-PAGE.

Biological Activity

ACE2 activity was measured by its binding ability in a functional ELISA.

The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.

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Introduction
ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
Physical Appearance
Sterile Filtered clear solution.
Stability
ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C. The addition of 0.1% albmin is highly recommended for long term storage use.
Purification Method
Purified by Protein-G 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:

Protein A/G/L Recombinant

Product # :

PRO-1936

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Shipped at Room temp

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Description

Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

Source

Escherichia Coli.

Formulation

Protein- A/G/L was lyophilized without any additives.

Purity

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

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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.

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-D Human Recombinant

Apolipoprotein D, Apo-D, ApoD.

Product # :

CYT-547

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Apolipoprotein-D Human Recombinant His Tag fusion protein at C-terminus (7 highlighted a.a.) produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 174 amino acids and having a molecular mass of 19.82kDa. The protein a.a sequence corresponds to the UniProtKB/Swiss-Prot entry P05090.The Following gene modifications were made:Trp99His, Cys116Ser, Ile118Ser, Leu120Ser amino acids exchanges were introduced at the surface of Apolipoprotein-D to enhance the protein’s solubility and another three Leu23Pro, Pro133Val, Asn134Ala amino acids exchanges which facilitate its genetic manipulation. The Apolipoprotein-D is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 1mg/ml in 4mM KH2PO4, 16mM Na2HPO4 and 115mM NaCl pH 7.5.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue.
Synonyms
Apolipoprotein D, Apo-D, ApoD.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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
It is recommended to add deionized H2O to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter this product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
Background
Apolipoprotein-D Human Recombinant: Illuminating the Role of a Multifaceted Lipid-Binding Protein
Abstract:

Apolipoprotein-D (ApoD), a multifunctional lipid-binding protein, has emerged as a fascinating player in lipid metabolism and neuroprotection. This research paper aims to provide an insightful overview of ApoD human recombinant, exploring its physiological functions, production methods, and potential therapeutic applications. By unraveling the complexities of ApoD, we gain valuable insights into its role in lipid homeostasis and its potential as a therapeutic target for neurodegenerative diseases. This article presents a concise yet comprehensive analysis of ApoD, humanizing its significance in the context of human health.
Introduction:

Understanding the intricate mechanisms underlying lipid metabolism and neuroprotection is crucial for the development of novel therapeutic strategies. ApoD, a versatile protein expressed in various tissues, offers unique insights into these areas. This paper delves into the multifaceted nature of ApoD, shedding light on its significance in lipid homeostasis and neuronal health.
Structure and Function of Apolipoprotein-D:

ApoD exhibits a complex molecular structure, comprising distinct domains that facilitate its binding to lipids and other biomolecules. It engages in diverse functions, including lipid transport, antioxidant defense, and modulation of neuroinflammatory responses. The versatility of ApoD underscores its pivotal role in maintaining cellular and tissue integrity.
Regulation of Apolipoprotein-D Expression:

The expression of ApoD is subject to intricate regulatory mechanisms influenced by hormonal and environmental cues. Understanding the factors governing ApoD expression provides valuable insights into its physiological roles and potential therapeutic applications.
Apolipoprotein-D and Neurodegenerative Diseases:

Growing evidence implicates ApoD in neuroprotection, particularly in the context of neurodegenerative diseases. ApoD exhibits neuroprotective properties by modulating oxidative stress, lipid peroxidation, and inflammatory responses, making it an intriguing target for therapeutic interventions.
Production of Apolipoprotein-D Human Recombinant:

Advanced biotechnological approaches, including recombinant DNA technology and protein expression systems, enable the production of ApoD human recombinant. These methods facilitate large-scale production, purification, and characterization of ApoD, paving the way for potential therapeutic applications.
Therapeutic Potential of Apolipoprotein-D Human Recombinant:

Targeting ApoD holds promise for the development of therapeutics aimed at neurodegenerative diseases. Modulating ApoD expression or function may provide neuroprotection, enhance neuronal survival, and mitigate the progression of neurodegenerative disorders.
Conclusion:

Apolipoprotein-D human recombinant represents a captivating area of research, bridging the fields of lipid metabolism and neurodegeneration. Understanding the intricate interplay between ApoD, lipid homeostasis, and neuroprotection is crucial for unraveling its full therapeutic potential. Continued investigation into the functions and mechanisms of ApoD will likely lead to novel therapeutic strategies for neurodegenerative diseases.
What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 19.82kDa.

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

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

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

What is the amino acid sequence of APO D Protein?
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.

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

What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D 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:

Human Clusterin

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

Product # :

CYT-548

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Source

Plasma.

Formulation

Human native Clusterin was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.1M phosphate buffer, 0.15M NaCl pH 7.5.

Purity

Greater than 95% as determined by SDS PAGE.

More Info

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, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Clusterin 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
It is recommended to add deionized H2O to prepare a working stock solution of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

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:

Actinin Alpha

Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

Product # :

PRO-518

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Description

Ultra pure Alpha Actinin having a Molecular mass of 95,000 Dalton.

Source

Chicken Gizzard.

Formulation

The protein was lyophilized from a 1mg/ml solution containing 10mM Tris acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, and 20mM NaCl.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

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Introduction
ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.
Synonyms
Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized a-Actinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution a-Actinin 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 a-Actinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Applications
Protein standard in 1D and 2D SDS gelelectrophoresis
Immunoassays
Immunization.

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:

Adiponectin Mouse Recombinant, His Tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-537

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Description

The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.

Source

Escherichia Coli.

Formulation

Acrp30 Mouse is a sterile filtered liquid formulation containing (1mg/ml) 20mM Tris-HCl pH-8, 1mM DTT and 10% Glycerol.

Purity

Acrp30 Mouse purity is greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 27.2kDa.

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

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MGSSHHHHHH SSGLVPRGSH MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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:

Omentin 298 a.a. Human Recombinant

Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

Product # :

CYT-061

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Description

Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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
MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR

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:

Mannose-Binding Lectin 2 Human Recombinant

COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.

Product # :

PRO-1285

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Description

MBL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (108-248) and having a molecular mass of 18 kDa. MBL2 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MBL2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M Nacl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.
Synonyms
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
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 MGSAASERKA LQTEMARIKK WLTFSLGKQV GNKFFLTNGE IMTFEKVKAL CVKFQASVAT PRNAAENGAI QNLIKEEAFL GITDEKTEGQ FVDLTGNRLT YTNWNEGEPN NAGSDEDCVL LLKNGQWNDV PCSTSHLAVC EFPI.

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:

Maltose Binding Protein E.coli Recombinant, His Tag

Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

Product # :

PRO-2322

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Description

Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

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-A Tilapia Recombinant

Product # :

CYT-1109

Price :

Quantity :

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Description

Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

Purity

Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia 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-A Tilapia in sterile water or 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 first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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:

Alpha-Fetoprotein Human

Alpha-fetoprotein, Alpha-fetoglobulin, Alpha-1-fetoprotein, AFP, FETA, HPAFP.

Product # :

PRO-406

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Description

Human alpha-fetoprotein purified from pooled human cord serum.

Source

Human cord serum.

Formulation

AFP protein filtered (0.2µm) solution in Tris buffered saline pH 7.5 and less than 0.1% NaN3.

Purity

Greater than 95%.

More Info

Introduction
AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Synonyms
Alpha-fetoprotein, Alpha-fetoglobulin, Alpha-1-fetoprotein, AFP, FETA, HPAFP.
Physical Appearance
Sterile Filtered clear solution.
Stability
Human Alpha-Fetoprotein should be stored at 2-8°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.

Description:

Calbindin-2 Human Recombinant

Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

Product # :

PRO-401

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Description

CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.
Synonyms
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
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 MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.

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:

Adiponectin glycosylated Human Recombinant, HMW Rich

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-764

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.

Source

HEK293.

Formulation

Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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:

Apolipoprotein-H Human Recombinant

Beta-2-glycoprotein 1, APC inhibitor, Activated protein C-binding protein, Anticardiolipin cofactor, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH, B2G1, BG, B2GP1.

Product # :

CYT-189

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Description

APOH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (20-345 a.a.) and having a molecular mass of 38.6kDa.APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APOH protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Synonyms
Beta-2-glycoprotein 1, APC inhibitor, Activated protein C-binding protein, Anticardiolipin cofactor, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH, B2G1, BG, B2GP1.
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 MGSGRTCPKP DDLPFSTVVP LKTFYEPGEE ITYSCKPGYV SRGGMRKFIC PLTGLWPINT LKCTPRVCPF AGILENGAVR YTTFEYPNTI SFSCNTGFYL NGADSAKCTE EGKWSPELPV CAPIICPPPS IPTFATLRVY KPSAGNNSLY RDTAVFECLP QHAMFGNDTI TCTTHGNWTK LPECREVKCP FPSRPDNGFV NYPAKPTLYY KDKATFGCHD GYSLDGPEEI ECTKLGNWSA MPSCKASCKV PVKKATVVYQ GERVKIQEKF KNGMLHGDKV SFFCKNKEKK CSYTEDAQCI DGTIEVPKCF KEHSSLAFWK TDASDVKPC.
Background
Apolipoprotein-H Human Recombinant: Unleashing the Potential for Cardiovascular Health
Abstract:
Apolipoprotein-H (Apo-H) is a remarkable protein with diverse functions in lipid metabolism and thrombotic regulation. This research paper provides an in-depth analysis of Apo-H human recombinant, exploring its physiological roles, genetic implications, and potential therapeutic applications. Understanding the intricacies of Apo-H sheds light on its significance in cardiovascular health and highlights its potential as a therapeutic target. This article offers a concise yet comprehensive examination of Apo-H, emphasizing its impact on human well-being.
Introduction:
Cardiovascular health is of utmost importance in preventing and managing cardiovascular diseases. Apo-H, a multifunctional protein involved in lipid metabolism and thrombotic regulation, offers a unique perspective in understanding these processes. This paper explores the multifaceted nature of Apo-H, elucidating its genetic implications and its role as a potential guardian of cardiovascular well-being.
Structure and Function of Apolipoprotein-H:
Apo-H possesses a complex molecular structure, consisting of distinct domains that facilitate interactions with lipoproteins and coagulation factors. It plays a critical role in lipid transport, regulating triglyceride-rich lipoproteins. Additionally, Apo-H contributes to the delicate balance of thrombotic processes through its anticoagulant and fibrinolytic activities.
Genetic Implications of Apolipoprotein-H:
The APOH gene, responsible for encoding Apo-H, exhibits genetic variations that can influence an individual's susceptibility to cardiovascular diseases. Understanding these genetic variations helps identify potential risk factors and therapeutic targets for cardiovascular disorders.
Apolipoprotein-H and Cardiovascular Diseases:
Apo-H has garnered significant attention in the field of cardiovascular diseases, particularly in relation to atherosclerosis and thrombotic events. Its versatility allows modulation of inflammatory responses, maintenance of endothelial function, and regulation of coagulation pathways. Investigating the intricate interplay between Apo-H and cardiovascular processes may yield innovative therapeutic strategies.
Production of Apolipoprotein-H Human Recombinant:
Cutting-edge biotechnological techniques, such as recombinant DNA technology and protein expression systems, enable the production of Apo-H human recombinant. These methods facilitate large-scale production, purification, and characterization of Apo-H, providing opportunities for potential therapeutic applications.
Therapeutic Potential of Apolipoprotein-H Human Recombinant:
Leveraging the therapeutic potential of Apo-H holds promise in cardiovascular interventions. Strategies aimed at enhancing Apo-H expression or function may contribute to lipid homeostasis, prevent thrombotic events, and reduce the risk of cardiovascular diseases.
Conclusion:
Apolipoprotein-H human recombinant represents a fascinating area of research, bridging the realms of lipid metabolism and cardiovascular health. Understanding the genetic implications and cardiovascular protective properties of Apo-H is pivotal in advancing our knowledge and developing novel therapeutic approaches for cardiovascular diseases. Continued investigation into the functions and mechanisms of Apo-H will likely unveil innovative strategies for promoting cardiovascular well-being.
What is the molecular weight/Mw of APOH Protein?
APOH Protein has a total Mw of 38.6kDa.

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

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

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

What is the amino acid sequence of APOH Protein?
MGSSHHHHHH SSGLVPRGSH MGSGRTCPKP DDLPFSTVVP LKTFYEPGEE ITYSCKPGYV SRGGMRKFIC PLTGLWPINT LKCTPRVCPF AGILENGAVR YTTFEYPNTI SFSCNTGFYL NGADSAKCTE EGKWSPELPV CAPIICPPPS IPTFATLRVY KPSAGNNSLY RDTAVFECLP QHAMFGNDTI TCTTHGNWTK LPECREVKCP FPSRPDNGFV NYPAKPTLYY KDKATFGCHD GYSLDGPEEI ECTKLGNWSA MPSCKASCKV PVKKATVVYQ GERVKIQEKF KNGMLHGDKV SFFCKNKEKK CSYTEDAQCI DGTIEVPKCF KEHSSLAFWK TDASDVKPC.

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

What is the endotoxin level for APOH Protein?
The endotoxin level is minimal, APOH 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:

Prohibitin Human Recombinant

PHB1, Prohibitin.

Product # :

PRO-1381

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Description

PHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-272a.a) and having a molecular mass of 31.9kDa. PHB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

PHB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Prohibitin (PHB) is an evolutionarily conserved gene that is ubiquitously expressed and which Mutations have been linked to sporadic breast cancer. PHB is thought to be a negative regulator of cell proliferation and may be a tumor suppressor. Prohibitin is expressed as two transcripts with changeable lengths of 3' untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, proposing that this longer 3' untranslated region functions as a trans-acting regulatory RNA.
Synonyms
PHB1, Prohibitin.
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 MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ.

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:

Alpha & Gamma-Adaptin Binding Protein Human Recombinant

P34, Alpha- and gamma-adaptin-binding protein p34.

Product # :

PRO-1479

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Description

AAGAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 36.7kDa.AAGAB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.
Synonyms
P34, Alpha- and gamma-adaptin-binding protein p34.
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 MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG GDRDEIEGLS SDEEH.

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:

Prohibitin 2 Human Recombinant

BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

Product # :

PRO-1533

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Description

PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PHB2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.
Synonyms
BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.
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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.

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 Super Antagonist Human Recombinant

Product # :

CYT-1238

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Shipped at Room temp

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Description

Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1mg/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 super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C 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 Super Leptin Antagonist 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-Gln.
Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

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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