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Description:

Activin-B Human Recombinant

Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

Product # :

CYT-058

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Shipped at Room temp

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Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana plant

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Purity

Greater than 97.0% as determined by Analysis 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 beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
Background
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.

What is the source or expression system of Activin B Protein?
Nicotinia

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

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

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

What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

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 Human Recombinant, Sf9

Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

Product # :

CYT-1002

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Description

Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.
Synonyms
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
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
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.9kDa.

What is the source or expression system of ADIPONECTIN Protein?
Sf9, Baculovirus cells.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% 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?
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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:

Allograft Inflammatory Factor 1 Human Recombinant

AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.

Product # :

CYT-697

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Shipped with Ice Packs

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Description

AIF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.9kDa. AIF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E. Coli.

Formulation

The AIF1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 200mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS PAGE.

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Introduction
Human AIF1 protein shares 98% homology/identity with that of rat. AIF1 is expressed in macrophages and neutrophils. The expression of AIF1 transcripts is upregulated by IFN-g in rat macrophages. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. In quiescent cultured human vascular smooth muscle cells synthesis of AIF1 is induced by IFN-g, IL1b, and conditioned medium of T-cells. Overexpression of AIF1 in human VSMCs results in enhanced growth of these cells. AIF1 is expressed during apoptosis rat mammary gland and ventral prostate tissues. Allograft Inflammatory Factor 1 is expressed by several tumor-associated activated macrophages and microglial cells in rat and human gliomas. There is an evident relationship of AIF1-expressing activated macrophages and microglial cells with tumor malignancy in humans.
Synonyms
AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.
Stability
Store AIF1 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 MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.
Background
Allograft Inflammatory Factor 1 Human Recombinant: Uncovering its Role in Immune Responses and Therapeutic Prospects
1. Abstract
This paper explores the Allograft Inflammatory Factor 1 Human Recombinant (AIF-1), a cytoplasmic, IFN-gamma-inducible calcium-binding protein involved in inflammation and immunity. We review the structure, biological roles, and involvement of AIF-1 in disease pathology. The therapeutic potential of AIF-1 in immune-related disorders is also explored.
2. Introduction
AIF-1, also known as IBA1, plays an important role in immune responses. It is associated with various immune cells, particularly macrophages, and has been implicated in numerous inflammatory and immune-related diseases. Understanding the function of AIF-1 could aid the development of novel therapeutic strategies.
3. Structure and Signaling of AIF-1
AIF-1 is a small 17 kDa protein with an EF-hand calcium-binding motif. Although the precise mechanism by which AIF-1 exerts its functions is not entirely clear, it is known to regulate the activation, migration, and proliferation of macrophages, key cells involved in immune responses.
4. Biological Functions of AIF-1
AIF-1 has been shown to play key roles in macrophage activation and function, which are central to inflammation and immunity. It is also implicated in cell survival, proliferation, and differentiation.
5. AIF-1 in Disease Pathology
AIF-1 has been associated with a range of inflammatory and immune-related diseases, including rheumatoid arthritis, atherosclerosis, and multiple sclerosis. It is also implicated in several cancers, further underscoring its broad physiological and pathological relevance.
6. Therapeutic Potential of AIF-1
Given its pivotal role in immune responses, AIF-1 presents an intriguing target for therapeutic interventions in immune-related diseases. Modulating the activity of AIF-1 could potentially alleviate pathological inflammation and autoimmunity.
7. Conclusion and Future Perspectives
Our knowledge of AIF-1 and its functions has significantly improved in recent years, but much remains to be discovered. Further research into AIF-1's exact molecular mechanisms and roles in disease will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1 Protein?
AIF1 Protein has a total Mw of 18.9kDa.

What is the source or expression system of AIF1 Protein?
Escherichia Coli.

What is the Purity of AIF1 Protein?
AIF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AIF1 Protein?
The biological functionality of AIF1 Protein will be determined in the future.

What is the amino acid sequence of AIF1 Protein?
MGSSHHHHHH SSGLVPRGSH MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.

What applications can AIF1 Protein be used in?
AIF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIF1 Protein?
The endotoxin level is minimal, AIF1 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:

Adiponectin Globular Recombinant, His Tag

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

Product # :

CYT-277

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Shipping Method :

Shipped at Room temp

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Description

Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).

Source

Escherichia Coli.

Formulation

Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.

Purity

Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.

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Introduction
Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Stability
For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.
Amino Acid Sequence
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% 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?
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

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:

Adiponectin (108-244 a.a.) Human Recombinant

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

Product # :

CYT-073

Price :

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Shipping Method :

Shipped with Ice Packs

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Description

Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by 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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% 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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..

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:

Adiponectin Mouse Recombinant, His Tag

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

Product # :

CYT-537

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Quantity :

Shipping Method :

Shipped with Ice Packs

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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.

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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:

Adiponectin Human Recombinant, HEK

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

Product # :

CYT-434

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 (Human Embryonic Kidney cell line).

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

Purity

Greater than 98% as determined by HPLC and SDS PAGE.

Biological Activity

In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

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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
White lyophilized (freeze-dried) powder.
Stability
For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.

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

What is the Purity of adiponectin Protein?
adiponectin Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

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:

Adipogenesis Associated, Mth938 Domain Containing Human Recombinant

Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

Product # :

PRO-2116

Price :

Quantity :

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Description

AAMDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122 a.a) and having a molecular mass of 15.7 kDa.AAMDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AAMDC protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Adipogenesis Associated, Mth938 Domain Containing, also known as AAMDC is a member of the AAMDC family and takes part in preadipocyte differentiation andadipogenesis.
Synonyms
Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.
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 MGSMTSPEIA SLSWGQMKVK GSNTTYKDCK VWPGGSRTWD WRETGTEHSP GVQPADVKEV VEKGVQTLVI GRGMSEALKV PSSTVEYLKK HGIDVRVLQT EQAVKEYNAL VAQGVRVGGV FHSTC.

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:

Actv Receptor Type 2A Human Recombinant

ACVR2A, ACTRIIA, ACTR-IIA,

Product # :

CYT-976

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Description

ACVR2A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids (20-135a.a.) and having a molecular mass of 14.4kDa (Molecular size on SDS-PAGE will appear at approximately 28kDa.ACVR2A is fused to 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ACVR2A protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
ACVR2A takes part in various biological processes including mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, carcinogenesis, and inflammation. ACVR2A which is a receptor for Actv A, Actv B and inhibin A mediates induction of adipogenesis by GDF6.
Synonyms
ACVR2A, ACTRIIA, ACTR-IIA,
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
AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.
Background
A Comprehensive Examination of the Activin Receptor Type 2A Human Recombinant: Biological Functions and Therapeutic Possibilities
1. Abstract
This paper delves into the complex world of Activin Receptor Type 2A Human Recombinant (ACVR2A), a crucial element of the Transforming Growth Factor-beta (TGF-beta) signaling pathway. The structure, biological implications, and signaling pathway of ACVR2A are all extensively reviewed. The potential for ACVR2A as a therapeutic target in various pathological conditions is also explored.
2. Introduction
The ACVR2A, a receptor protein vital to the TGF-beta signaling pathway, plays a significant role in a multitude of biological processes, including embryogenesis, cell differentiation, and homeostasis. Understanding the intricate operations of ACVR2A could open the door to innovative therapeutic strategies.
3. Structure and Signaling of ACVR2A
As a transmembrane serine/threonine kinase receptor, ACVR2A is characterized by a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Upon binding of specific ligands like activin, ACVR2A interacts with type I receptors to trigger phosphorylation events, leading to the activation of downstream SMAD signaling pathways.
4. Biological Functions of ACVR2A
ACVR2A plays a substantial role in a wide range of biological processes. These include embryonic development, cell differentiation, bone growth, immune responses, and homeostasis. Furthermore, ACVR2A is instrumental in follicle-stimulating hormone (FSH) regulation, highlighting its importance in reproduction.
5. ACVR2A in Disease Pathology
Impairments in ACVR2A signaling have been linked to several diseases, including various cancers and reproductive disorders. Mutations in the ACVR2A gene have been implicated in tumor progression, underscoring the receptor's role in cell proliferation and differentiation.
6. Therapeutic Potential of ACVR2A
The centrality of ACVR2A in critical biological processes and disease pathology suggests its therapeutic potential. By modulating ACVR2A signaling, it may be possible to intervene in diseases characterized by aberrant TGF-beta signaling. Additionally, ACVR2A antagonists are being studied for their potential in cancer treatment.
7. Conclusion and Future Perspectives
Our comprehension of ACVR2A's functions has substantially increased in recent years, yet much remains to be discovered. Further research into ACVR2A's precise molecular mechanisms and involvement in disease will undoubtedly yield new therapeutic strategies.
What is the molecular weight / Mw of ACVR2A Protein?
ACVR2A Protein has a total Mw of 14.4kDa.
What is the source or expression system of ACVR2A Protein?
Sf9, Baculovirus cells.

What is the Purity of ACVR2A Protein?
ACVR2A Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ACVR2A Protein?
The biological functionality of ACVR2A Protein will be determined in the future.

What is the amino acid sequence of ACVR2A Protein?
AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

What applications can ACVR2A Protein be used in?
ACVR2A Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ACVR2A Protein?
The endotoxin level is minimal, ACVR2A 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:

Adiponectin (72-244) Human Recombinant

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

Product # :

CYT-1231

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Description

The Adiponectin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 24kDa protein containing 173 amino acid residues of the Acrp30 Human, 72-244 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Adiponectin 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 water to prepare a working stock solution of approximately 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 on cell culture.
Amino Acid Sequence
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN
Background
Adiponectin is a protein produced and secreted by adipose tissue. Adiponectin takes part in regulating glucose levels as well as fatty acid breakdown.
Adiponectin ‘s Functions:
Anti-Inflammatory Effects - Adiponectin has anti-inflammatory properties that helps mitigate chronic inflammation.
Regulation of Glucose and Lipid Metabolism - Adiponectin Enhances insulin sensitivity, helping in regulation of blood sugar levels and also promotes fatty acid oxidation, which helps reduce fat accumulation.
Cardiovascular Health - It may influence vascular health and is associated with a lower risk of cardiovascular diseases.
Levels and Health Implications:
Normal Levels - usually, higher levels of adiponectin are associated with a lower risk of metabolic syndrome, cardiovascular diseases and type 2 diabetes.
Low Levels - Reduced adiponectin levels are often linked with obesity, insulin resistance, and other metabolic disorders.
Factors Influencing on the Adiponectin Levels:
Weight - High body fat (especially visceral fat) can lower adiponectin levels.
Diet and Exercise - Regular physical activity and a healthy diet can increase adiponectin levels.
Genetics - Genetic factors might also be an influence on an individual adiponectin level.
Adiponectin is an important component in metabolic health, therefore continuing the research of its functions and regulation keeps advance our understanding of its role in diseases like diabetes and cardiovascular conditions.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTINProtein 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?
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN.

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:

Sorbin And SH3 Domain Containing 3 Human Recombinant

Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

Product # :

PRO-1829

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Description

SORBS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.1 kDa. SORBS3 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The SORBS3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.
Synonyms
Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.
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 MGSMADGGSP FLGRRDFVYP SSTRDPSASN GGGSPARREE KKRKAARLKF DFQAQSPKEL TLQKGDIVYI HKEVDKNWLE GEHHGRLGIF PANYVEVLPA DEIPKPIKPP TYQVLEYGEA VAQYTFKGDL EVELSFRKGE HICLIRKVNE NWYEGRITGT GRQGIFPASY VQVSREPRLR LCDDGPQLPT SPRLTAAARS ARHPSSPSAL RSPADPIDLG GQTSPRRTGF SFPTQEPRPQ TQNLGTPGPA LSHSRGPSHP LDLGTSSPNT SQIHWTPYRA MYQYRPQNED ELELREGDRV DVMQQCDDGW FVGVSRRTQK FGTFPGNYVA PV

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:

APAF1 interacting protein Human Recombinant

APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.

Product # :

PRO-1186

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APIP Human Recombinant produced E. coli is a single polypeptide chain containing 266 amino acids (1-242) and having a molecular mass of 29.7kDa.APIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The APIP solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
APIP catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). APIP has an anti-apoptotic function and inhibits muscle ischemic impairment. APIP inhibits the cytochrome c-dependent and APAF1-mediated cell death.
Synonyms
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
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 MGSHMSGCDA REGDCCSRRC GAQDKEHPRY LIPELCKQFY HLGWVTGTGG GISLKHGDEI YIAPSGVQKE RIQPEDMFVC DINEKDISGP SPSKKLKKSQ CTPLFMNAYT MRGAGAVIHT HSKAAVMATL LFPGREFKIT HQEMIKGIKK CTSGGYYRYD DMLVVPIIEN TPEEKDLKDR MAHAMNEYPD SCAVLVRRHG VYVWGETWEK AKTMCECYDY LFDIAVSMKK VGLDPSQLPV GENGIV

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:

Acyl-CoA Dehydrogenase, Very Long Chain Human Recombinant

ACAD6, LCACD, VLCAD.

Product # :

ENZ-250

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Description

ACADVL Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 636 amino acids (41-655 a.a.) and having a molecular mass of 68.5 kda. ACADVL contains 21 amino acid His-Tag at the N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, 1mM EDTA, 10% glycerol and 100mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ACADVL is an inner mitochondrial membrane enzyme that is part of the family of acyl-CoA dehydrogenases. ACADVL protein participates in lipid metabolism and has catalytic activity toward esters of long chain and very long chain fatty acids such as palmitoyl-CoA and stearoyl-CoA, and is involved in the first step of the fatty acid β-oxidation pathway. ACADVL deficiency in reduces myocardial fatty acid beta-oxidation and is related with cardiomyopathy.
Synonyms
ACAD6, LCACD, VLCAD.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store ACADVL 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 MAGGAAQLAL DKSDSHPSDA LTRKKPAKAE SKSFAVGMFK GQLTTDQVFP YPSVLNEEQT QFLKELVEPV SRFFEEVNDP AKNDALEMVE ETTWQGLKEL GAFGLQVPSE LGGVGLCNTQ YARLVEIVGM HDLGVGITLG AHQSIGFKGI LLFGTKAQKE KYLPKLASGE TVAAFCLTEP SSGSDAASIR TSAVPSPCGK YYTLNGSKLW ISNGGLADIF TVFAKTPVTD PATGAVKEKI TAFVVERGFG GITHGPPEKK MGIKASNTAE VFFDGVRVPS ENVLGEVGSG FKVAMHILNN GRFGMAAALA GTMRGIIAKA VDHATNRTQF GEKIHNFGLI QEKLARMVML QYVTESMAYM VSANMDQGAT DFQIEAAISK IFGSEAAWKV TDECIQIMGG MGFMKEPGVE RVLRDLRIFR IFEGTNDILR LFVALQGCMD KGKELSGLGS ALKNPFGNAG LLLGEAGKQL RRRAGLGSGL SLSGLVHPEL SRSGELAVRA LEQFATVVEA KLIKHKKGIV NEQFLLQRLA DGAIDLYAMV VVLSRASRSL SEGHPTAQHE KMLCDTWCIE AAARIREGMA ALQSDPWQQE LYRNFKSISK ALVERGGVVT SNPLGF.

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:

Activin-A Rat Recombinant

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-147

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Description

Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.

What is the source or expression system of Activin A Protein?
Ecoli

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

What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

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

What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

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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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.

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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; 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:

Adiponectin Mouse Recombinant, Trimeric form

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

Product # :

CYT-247

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

Source

HEK293 (Human embryonic kidney cell line).

Formulation

Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

Purity

Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse 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 deionized water to prepare a working stock solution of approximately 0.5 mg/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.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.

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

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% 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 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:

Activin-B Human Recombinant, Active

Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

Product # :

CYT-057

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Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana plant

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Purity

Greater than 97.0% as determined by Analysis by SDS-PAGE.

Biological Activity

The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.
Background
An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active
1. Abstract
Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.
2. Introduction
The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.
3. Structure and Synthesis of Activin-B
Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.
4. Biological Functions of Activin-B
Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.
5. Activin-B in Regenerative Medicine
Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.
6. Activin-B and Reproductive Health
Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.
7. Activin-B in Cancer
Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.
8. Conclusion and Future Perspectives
Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.
What is the source or expression system of Activin B Protein?
Nicotinia

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

What is the Biological Activity of Activin B Protein?
The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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

What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

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:

Ephrin A5 Human Recombinant

EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.

Product # :

PRO-2327

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Shipped with Ice Packs

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Description

EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EFNA5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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:

Globular Adiponectin Mouse Recombinant

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

Product # :

CYT-432

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

The globular domain of Adiponectin Mouse Recombinant / Acrp30 Mouse contains 138 amino acid residues from a.a. 111-247 having molecular mass of 16 kDa was over expressed in E.coli and purified by using conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

Acrp30 Mouse (1mg/ml) solution containing 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Introduction
Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16kDa.

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

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% 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?
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN

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:

Energy Homeostasis Associated Human Recombinant

Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

Product # :

PRO-1569

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

Source

Escherichia Coli.

Formulation

ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.
Synonyms
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
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 water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ENHO is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

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:

Allograft Inflammatory Factor 1 Like Human Recombinant

Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.

Product # :

CYT-007

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

AIF1L produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150a.a.) and having a molecular mass of 19.2kDa.AIF1L is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIF1L protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

sds-page

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Synonyms
Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.
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 MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.
Background
Allograft Inflammatory Factor 1-Like Human Recombinant: Investigating its Role in Immune Responses and Potential Therapeutic Applications
1. Abstract
This paper seeks to provide an in-depth overview of Allograft Inflammatory Factor 1-Like Human Recombinant (AIF-1L), a significant protein involved in the regulation of inflammatory responses. By delving into the structure, biological functions, and pathological implications of AIF-1L, we attempt to shed light on its potential as a therapeutic target in immune-mediated disorders.
2. Introduction
AIF-1L belongs to the allograft inflammatory factor protein family and is implicated in immune responses. With its intricate interaction with a multitude of immune cells and involvement in various inflammatory and immune-related diseases, it serves as a pivotal point of interest for therapeutic intervention research.
3. Structure and Signaling of AIF-1L
AIF-1L shares a conserved EF-hand calcium-binding motif with its counterpart AIF-1, suggesting similar calcium-dependent activities. While its signaling pathway remains largely elusive, the protein is believed to modulate macrophage activation, an integral part of immune response regulation.
4. Biological Functions of AIF-1L
AIF-1L is fundamentally involved in immune response modulation, especially in the context of macrophage activation. It plays key roles in managing inflammation, cell proliferation, survival, and differentiation.
5. AIF-1L in Disease Pathology
AIF-1L is linked with a range of inflammatory and immune-related disorders, including but not limited to rheumatoid arthritis, atherosclerosis, and certain cancers. This association underscores its profound physiological relevance and potential as a therapeutic target.
6. Therapeutic Potential of AIF-1L
Given its central role in immune responses, AIF-1L presents a promising target for therapeutic strategies. Manipulating AIF-1L activity could pave the way for novel treatments of various inflammatory and immune-mediated diseases.
7. Conclusion and Future Perspectives
Though our comprehension of AIF-1L has made significant strides, there is still much terrain left to explore. Future research directed at the precise molecular mechanisms and pathological roles of AIF-1L will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1L Protein?
AIF1L Protein has a total Mw of 19.2kDa.

What is the source or expression system of AIF1L Protein?
Escherichia Coli.

What is the Purity of AIF1L Protein?
AIF1L Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AIF1L Protein?
The biological functionality of AIF1L Protein will be determined in the future.

What is the amino acid sequence of AIF1L Protein?
MGSSHHHHHH SSGLVPRGSH MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.

What applications can AIF1L Protein be used in?
AIF1L Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIF1L Protein?
The endotoxin level is minimal, AIF1L 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-J Mouse Recombinant

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

Product # :

CYT-1172

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.

Source

HEK293

Formulation

Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Clusterin also known as 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 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -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.
Clusterin is up/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 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 water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 50.2kDa.

What is the source or expression system of CLUSTERIN Protein?
HEK293

What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >90% 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?
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

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:

Activin-A Mouse Recombinant

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-146

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 10⁵ units/mg.

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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli

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

What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 units/mg.

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

What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

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:

Myozenin 1 Human Recombinant

CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.

Product # :

PRO-1652

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Citations

Description

MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.

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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